Protein Variants | Comment | Organism |
---|---|---|
additional information | in DELTAndhD1 and DELTAndhD1/D2 mutants, the NDH-1L complex is missing but NDH-1M and NDH-1S are abundant in low-CO2 conditions. The DELTAndhD3 and DELTAndhD3/D4 mutants lack NDH-1S but exhibit wild-type levels of NDH-1M at low CO2. In both mutants, the carbon uptake is impaired and more severely in the double mutant that can grow at low CO2 only at elevated pH (pH 8.3 but not 7.5), when other mechanisms of carbon uptake are activated. Deletion of the small hydrophobic NdhL subunit is not essential for the assembly of NDH-1L and NDH-1M. This subunit might be important in supporting a specific conformation of the NDH-1 complexes because the importance of NdhL for the function in CO2 uptake is unambiguously demonstrated | Synechocystis sp. 6803 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | all NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helixes | Thermosynechococcus vestitus | - |
- |
additional information | all NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helixes | Nostoc sp. PCC 7120 = FACHB-418 | - |
- |
additional information | all NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helixes | Synechocystis sp. 7942 | - |
- |
additional information | all NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helixes | Synechocystis sp. 7002 | - |
- |
additional information | in Synechocystis sp. and in Anacystis nidulans, subunits NdhJ and NdhK are found in both the plasma membrane and the thylakoid membrane. All NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helices | Synechococcus elongatus PCC 7942 = FACHB-805 | - |
- |
additional information | in Synechocystis sp. and in Anacystis nidulans, subunits NdhJ and NdhK are found in both the plasma membrane and the thylakoid membrane. All NdhF, NdhD proteins and NdhB contain 12-17 transmembrane helixes | Synechocystis sp. 6803 | - |
- |
plasma membrane | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | 5886 | - |
plasma membrane | - |
Synechocystis sp. 6803 | 5886 | - |
plasma membrane | Anabaena sp. PCC 7120, the NDH-1 complex is localized to the plasma membrane only | Nostoc sp. PCC 7120 = FACHB-418 | 5886 | - |
thylakoid membrane | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | 42651 | - |
thylakoid membrane | - |
Thermosynechococcus vestitus | 42651 | - |
thylakoid membrane | - |
Synechocystis sp. 7942 | 42651 | - |
thylakoid membrane | - |
Synechocystis sp. 7002 | 42651 | - |
thylakoid membrane | - |
Synechocystis sp. 6803 | 42651 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Synechococcus elongatus PCC 7942 = FACHB-805 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Thermosynechococcus vestitus | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Nostoc sp. PCC 7120 = FACHB-418 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Synechocystis sp. 7942 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Synechocystis sp. 7002 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Synechocystis sp. 6803 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nostoc sp. PCC 7120 = FACHB-418 | - |
- |
- |
Synechococcus elongatus PCC 7942 = FACHB-805 | - |
- |
- |
Synechocystis sp. 6803 | - |
- |
- |
Synechocystis sp. 7002 | - |
- |
- |
Synechocystis sp. 7942 | - |
- |
- |
Thermosynechococcus vestitus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
in the NDH-1 complex, the interactions between the connecting and membrane core domains seem to be strong enough to keep them together during solubilization | Thermosynechococcus vestitus |
in the NDH-1 complex, the interactions between the connecting and membrane core domains seem to be strong enough to keep them together during solubilization | Synechocystis sp. 6803 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Thermosynechococcus vestitus | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Nostoc sp. PCC 7120 = FACHB-418 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Synechocystis sp. 7942 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Synechocystis sp. 7002 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Synechocystis sp. 6803 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cyanobacterial NDH-1 complex | - |
Synechococcus elongatus PCC 7942 = FACHB-805 |
cyanobacterial NDH-1 complex | - |
Thermosynechococcus vestitus |
cyanobacterial NDH-1 complex | - |
Nostoc sp. PCC 7120 = FACHB-418 |
cyanobacterial NDH-1 complex | - |
Synechocystis sp. 7942 |
cyanobacterial NDH-1 complex | - |
Synechocystis sp. 7002 |
cyanobacterial NDH-1 complex | - |
Synechocystis sp. 6803 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Fe-S cluster | presence of several iron-sulfur clusters | Synechococcus elongatus PCC 7942 = FACHB-805 | |
Fe-S cluster | presence of several iron-sulfur clusters | Thermosynechococcus vestitus | |
Fe-S cluster | presence of several iron-sulfur clusters | Nostoc sp. PCC 7120 = FACHB-418 | |
Fe-S cluster | presence of several iron-sulfur clusters | Synechocystis sp. 7942 | |
Fe-S cluster | presence of several iron-sulfur clusters | Synechocystis sp. 7002 | |
Fe-S cluster | presence of several iron-sulfur clusters | Synechocystis sp. 6803 | |
Ferredoxin | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | |
Ferredoxin | - |
Thermosynechococcus vestitus | |
Ferredoxin | - |
Nostoc sp. PCC 7120 = FACHB-418 | |
Ferredoxin | - |
Synechocystis sp. 7942 | |
Ferredoxin | - |
Synechocystis sp. 7002 | |
Ferredoxin | - |
Synechocystis sp. 6803 | |
FMN | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | |
FMN | - |
Thermosynechococcus vestitus | |
FMN | - |
Nostoc sp. PCC 7120 = FACHB-418 | |
FMN | - |
Synechocystis sp. 7942 | |
FMN | - |
Synechocystis sp. 7002 | |
FMN | - |
Synechocystis sp. 6803 | |
plastoquinone | - |
Synechococcus elongatus PCC 7942 = FACHB-805 | |
plastoquinone | - |
Thermosynechococcus vestitus | |
plastoquinone | - |
Nostoc sp. PCC 7120 = FACHB-418 | |
plastoquinone | - |
Synechocystis sp. 7942 | |
plastoquinone | - |
Synechocystis sp. 7002 | |
plastoquinone | - |
Synechocystis sp. 6803 |
General Information | Comment | Organism |
---|---|---|
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Synechococcus elongatus PCC 7942 = FACHB-805 |
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Thermosynechococcus vestitus |
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Nostoc sp. PCC 7120 = FACHB-418 |
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Synechocystis sp. 7942 |
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Synechocystis sp. 7002 |
evolution | the ndhD and ndhF genes belong to a large family and might have appeared by ancient gene duplication events during evolution. NdhD1 and NdhF1 are present in all cyanobacteria sequenced so far, but the occurrence of other NdhD and NdhF genes varies among cyanobacteria. The ndhD1/ndhD2 and ndhF1 are related to chloroplast ndhD and ndhF genes, respectively, whereas the ndhD3/ndhD4 and ndhF3/ndhF4 types of genes are specific to cyanobacteria | Synechocystis sp. 6803 |
malfunction | inactivation of ndhB or ndhK results in a high-CO2-requiring phenotype. In cells of the ndhD1/D2 double mutant grown in high CO2, the cyclic electron flow around PSI is strongly impaired and the respiration activity is also low. But cells of this mutant grown at low CO2 show PSI cyclic electron flow similar to wild-type. The donation of electron from NADPH to plastoquinone occurs in thylakoid membranes of wild-type Synechocystis 6803 but is impaired in those of the NdhB-defective mutant | Synechocystis sp. 6803 |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain | Synechococcus elongatus PCC 7942 = FACHB-805 |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain | Thermosynechococcus vestitus |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain | Synechocystis sp. 7942 |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain | Synechocystis sp. 7002 |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain | Synechocystis sp. 6803 |
metabolism | reverse genetics and proteomics studies focussing on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake, overview. The NDH-1 complexes in cyanobacteria share a common NDH-1M core complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain. In Anabaena sp. PCC 7120, the NDH-1 complex is localized to the plasma membrane only | Nostoc sp. PCC 7120 = FACHB-418 |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Synechococcus elongatus PCC 7942 = FACHB-805 |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Thermosynechococcus vestitus |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Nostoc sp. PCC 7120 = FACHB-418 |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Synechocystis sp. 7942 |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Synechocystis sp. 7002 |
additional information | soluble and membrane-type subunits, composition of the NDH-1 complex types in cyanobacteria: Ndh-1L, Ndh-1M, and Ndh-1MS, complex structure and interactions, detailed overview | Synechocystis sp. 6803 |
physiological function | NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions | Synechococcus elongatus PCC 7942 = FACHB-805 |
physiological function | NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions | Thermosynechococcus vestitus |
physiological function | NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. NdhD1(D2)/NdhF1 are important for both respiration and cyclic electron flow, whereas NdhD3/NdhF3 are responsible for low-CO2-inducible, high-affinity CO2 uptake system, and NdhD4/NdhF4 is involved in a constitutive, low-affinity CO2 uptake. The roles of NdhD5 and NdhD6 are undetermined | Synechocystis sp. 7942 |
physiological function | NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. NdhD1(D2)/NdhF1 are important for both respiration and cyclic electron flow, whereas NdhD3/NdhF3 are responsible for low-CO2-inducible, high-affinity CO2 uptake system, and NdhD4/NdhF4 is involved in a constitutive, low-affinity CO2 uptake. The roles of NdhD5 and NdhD6 are undetermined | Synechocystis sp. 7002 |
physiological function | NDH-1/complex I is a multisubunit enzyme with the following characteristic features: the presence of flavin mononucleotide (FMN) and several iron-sulfur (Fe-S) clusters, sensitivity to rotenone or piericidin A, and an L-shaped structure with a membrane domain and a perpendicular peripheral domain composed of hydrophobic and hydrophilic subunits. In cyanobacteria, the NDH-1 complexes are involved in inorganic carbon-concentrating mechanisms, which are vitally important for aquatic phototrophs under carbon limitation in order to compensate for the relatively low affinity of their Rubisco for CO2. NDH-1 participates in cellular respiration and PSI cyclic electron flow in cyanobacteria, and the NdhB subunit is essential for both functions. Subunit NdhL plays an important role in CO2 uptake and is part of the Synechocystis NDH-1 complex. In contrast to the NdhB, NdhL and NdhK subunits, the ndhH gene is vital to the survival of Synechocystis 6803 even under high-CO2 growth conditions. NDH-1MS is also involved in cyclic electron flow | Synechocystis sp. 6803 |