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Information on EC 6.3.2.31 - coenzyme F420-0:L-glutamate ligase
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EC Tree
6.3.2.31 coenzyme F420-0:L-glutamate ligaseIUBMB Comments
This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the reaction described here the enzyme attaches a glutamate via its alpha-amine group to F420-0. In the second reaction (EC 6.3.2.34, coenzyme F420-1---gamma-L-glutamate ligase) it catalyses the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
mj0768, cofe-af, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional F420 biosynthesis protein FbiB
BQ2027_MB3290
FbiB
bifunctional F420 biosynthesis protein FbiB
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bifunctional F420 biosynthesis protein FbiB
Mycobacterium tuberculosis variant bovis ATCC BAA-935
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:coenzyme F420-0 ligase (GDP-forming)
This protein catalyses the successive addition of two glutamate residues to cofactor F420 by two distinct and independent reactions. In the reaction described here the enzyme attaches a glutamate via its alpha-amine group to F420-0. In the second reaction (EC 6.3.2.34, coenzyme F420-1---gamma-L-glutamate ligase) it catalyses the addition of a second L-glutamate residue to the gamma-carboxyl of the first glutamate.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate + ATP + coenzyme F420-0
ADP + phosphate + coenzyme F420-1
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-
-
?
L-glutamate + dGTP + coenzyme F420-0
dGDP + phosphate + coenzyme F420-1
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
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-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme F420-1
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
-
-
?
L-glutamate + UTP + coenzyme F420-0
UDP + phosphate + coenzyme F420-1
coenzyme F420-1 is coenzyme F420 with one glutamic acid residue attached via its alpha-NH2 to F420-0
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-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
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-
-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
reduced coenzyme F420 (F420H2) is the true substrate of F420-0-gamma-glutamyl ligase for the attachment of more than two glutamate residues to the coenzyme
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-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
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-
-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
reduced coenzyme F420 (F420H2) is the true substrate of F420-0-gamma-glutamyl ligase for the attachment of more than two glutamate residues to the coenzyme
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-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
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-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
the enzyme protein catalyzes two distinct and independent reactions, firstly attaching a glutamte via its alpha-NH2 to F420-0. The second reaction (cf. coenzyme F420-1:gamma-glutamyl ligase) is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
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-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
step in the biosynthesis of coenzyme F420
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-
?
additional information
?
-
CofE incubated with 10 mM beta-glutamate, D-glutamate, gamma-glutamylglutamate, DL-2-amino-3-phosphonopropionic acid, 2-carboxyethylphosphonic acid, or L-R-aminoadipic acid produces no F420-1
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-
?
additional information
?
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-
CofE incubated with 10 mM beta-glutamate, D-glutamate, gamma-glutamylglutamate, DL-2-amino-3-phosphonopropionic acid, 2-carboxyethylphosphonic acid, or L-R-aminoadipic acid produces no F420-1
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-
?
additional information
?
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full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides
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-
?
additional information
?
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F420H2 is the preferred substrate for the extension of glutamate chains of F420 by FbiB
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-
additional information
?
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full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides
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-
?
additional information
?
-
F420H2 is the preferred substrate for the extension of glutamate chains of F420 by FbiB
-
-
-
additional information
?
-
full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
reduced coenzyme F420 (F420H2) is the true substrate of F420-0-gamma-glutamyl ligase for the attachment of more than two glutamate residues to the coenzyme
-
-
?
GTP + coenzyme F420-0 + L-glutamate
GDP + phosphate + coenzyme F420-1
reduced coenzyme F420 (F420H2) is the true substrate of F420-0-gamma-glutamyl ligase for the attachment of more than two glutamate residues to the coenzyme
-
-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
the enzyme protein catalyzes two distinct and independent reactions, firstly attaching a glutamte via its alpha-NH2 to F420-0. The second reaction (cf. coenzyme F420-1:gamma-glutamyl ligase) is a gamma ligation, taking place when a certain amount of monoglutamylated F420-1 has accumulated
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-
?
L-glutamate + GTP + coenzyme F420-0
GDP + phosphate + coenzyme gamma-F420-1
step in the biosynthesis of coenzyme F420
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2
K+
CofE absolutely requires a monovalent cation for activity, the greatest extent of activation is achieved by K+, with maximum stimulation occurring at 0.2 M KCl, NH4+ stimulates activity to a lesser extent, extent, whereas Na+ and Li+ have no effect on CofE activity. A mixture of Mn2+, Mg2+, and K+ is the most effective
Mg2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
Mn2+
Na+
highest activity in presence of both Na+ and Mn2+, assay in presence of 100mMNaCl, 5mMMnCl2
NH4+
CofE absolutely requires a monovalent cation for activity, the greatest extent of activation is achieved by K+, NH4+ stimulates activity to a lesser extent, whereas Na+ and Li+ have no effect on CofE activity. A mixture of Mn2+, Mg2+, and K+ is the most effective
Mn2+
there are two Mn2+-binding sites per monomer within close proximity of the GDP alpha and beta-phosphate groups
Mn2+
divalent cation requirement, maximum CofE activity is observed with the addition of 10 mM MnCl2. The combination of 5 mM MgCl2 and 2-5 mM of MnCl2 supports the highest activity
Mn2+
highest activity in presence of both Na+ and Mn2+, assay in presence of 100mMNaCl, 5mMMnCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cs2+
in the presence of either Rb+ or Cs+ at 0.2 M concentration, the only product of reaction is F420-1
Rb+
in the presence of either Rb+ or Cs+ at 0.2 M concentration, the only product of reaction is F420-1
additional information
no significant inhibition when CofE is incubated with the following compound (10 mM): L-aspartate, Lglutamine, L-homocysteic acid, or DL-amino-4-phosphono-butyric acid
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additional information
-
no significant inhibition when CofE is incubated with the following compound (10 mM): L-aspartate, Lglutamine, L-homocysteic acid, or DL-amino-4-phosphono-butyric acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no change of CofE activity is observed when the enzyme is assayed with the addition of 10 mM dithiothreitol to the reaction mixture
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additional information
-
no change of CofE activity is observed when the enzyme is assayed with the addition of 10 mM dithiothreitol to the reaction mixture
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 80
35°C: about 30% of maximal activity, 80°C: about 55% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
physiological function
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
physiological function
in vitro, MtbFbiB synthesizes side chains containing up to seven glutamate residues if cofactor F420 is presented to the enzyme in a two-electron reduced state (F420H2). The polyglutamylation process requires the assistance of F420-dependent glucose-6-phosphate dehydrogenase (Fgd) which reduces F420 to F420H2. Starting with F420-0H2, the amino-terminal domain of FbiB may build F420-2H2, which is then transferred to the carboxy-terminal domain for further glutamylation. F420-2H2 modifies the carboxy-terminal domain structurally to accommodate longer glutamyl chains
physiological function
Mycobacterium tuberculosis variant bovis ATCC BAA-935
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both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
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physiological function
-
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
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physiological function
-
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
-
physiological function
-
in vitro, MtbFbiB synthesizes side chains containing up to seven glutamate residues if cofactor F420 is presented to the enzyme in a two-electron reduced state (F420H2). The polyglutamylation process requires the assistance of F420-dependent glucose-6-phosphate dehydrogenase (Fgd) which reduces F420 to F420H2. Starting with F420-0H2, the amino-terminal domain of FbiB may build F420-2H2, which is then transferred to the carboxy-terminal domain for further glutamylation. F420-2H2 modifies the carboxy-terminal domain structurally to accommodate longer glutamyl chains
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FBIB_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
448
0
47578
Swiss-Prot
-
FBIB_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
448
0
47578
Swiss-Prot
-
FBIB_MYCBT
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
448
0
47578
Swiss-Prot
-
FBIB_MYCPA
Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
449
0
47398
Swiss-Prot
-
FBIB_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
454
0
48567
Swiss-Prot
-
FBIB_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
448
0
47578
Swiss-Prot
-
FBIB_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
448
0
47578
Swiss-Prot
-
FBIB_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
448
0
47578
Swiss-Prot
-
FBIB_NOCFA
Nocardia farcinica (strain IFM 10152)
452
0
47993
Swiss-Prot
-
FBIB_STRAW
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
423
0
44673
Swiss-Prot
-
FBIB_STRCO
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
443
0
46867
Swiss-Prot
-
COFE_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
249
0
27261
Swiss-Prot
-
COFE_HALLT
Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)
251
0
27294
Swiss-Prot
-
COFE_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
257
0
27600
Swiss-Prot
-
COFE_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
253
0
26441
Swiss-Prot
-
COFE_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
253
0
26441
Swiss-Prot
-
COFE_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
254
0
27899
Swiss-Prot
-
COFE_METBF
Methanosarcina barkeri (strain Fusaro / DSM 804)
255
0
27853
Swiss-Prot
-
COFE_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
249
0
27148
Swiss-Prot
-
COFE_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
252
0
27135
Swiss-Prot
-
COFE_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
248
0
27042
Swiss-Prot
-
COFE_METM7
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
248
0
26957
Swiss-Prot
-
COFE_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
254
0
27741
Swiss-Prot
-
COFE_METMP
Methanococcus maripaludis (strain S2 / LL)
248
0
26989
Swiss-Prot
-
COFE_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
252
0
26538
Swiss-Prot
-
COFE_NATPD
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara)
253
0
27293
Swiss-Prot
-
A0A150J1L9_9EURY
252
0
27407
TrEMBL
-
A0A0F7P6W6_9EURY
253
0
26659
TrEMBL
-
A0A284VM82_9EURY
252
0
27823
TrEMBL
-
A0A811THJ2_9EURY
256
0
27378
TrEMBL
-
A0A7W2D800_9ACTN
437
0
46180
TrEMBL
-
A0A6I3ZMN5_9MYCO
454
0
48196
TrEMBL
-
A0A833DM14_9ARCH
212
0
22936
TrEMBL
-
A0A343TM23_9EURY
251
0
26839
TrEMBL
-
A0A7G9YPQ5_9EURY
249
0
26893
TrEMBL
-
A0A8D3WIH7_STRFA
Streptomyces pratensis (strain ATCC 33331 / IAF-45CD)
442
0
46381
TrEMBL
-
A0A7K1K4V1_9MYCO
451
0
47871
TrEMBL
-
A0A0E3SH00_9EURY
254
0
27924
TrEMBL
-
A0A841BSA1_9ACTN
254
0
26835
TrEMBL
-
K4RA92_STRDJ
Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
443
0
46561
TrEMBL
-
A0A087S3C5_9ARCH
255
0
28282
TrEMBL
-
A0A1V4U2Z2_9EURY
247
0
27356
TrEMBL
-
A0A2R6K8P4_9EURY
250
0
26772
TrEMBL
-
A0A2R6JHG2_9EURY
252
0
27333
TrEMBL
-
A0A7J3TXR5_9ARCH
251
0
27344
TrEMBL
-
A0A523ZKI5_9ARCH
252
0
27467
TrEMBL
-
A0A537H4M6_9ARCH
274
0
29276
TrEMBL
-
A0A537DFS4_9ARCH
291
0
32016
TrEMBL
-
A0A537EU02_9ARCH
254
0
27700
TrEMBL
-
A0A3R7BBP7_9ARCH
236
0
25775
TrEMBL
-
A0A523T2J2_9ARCH
273
0
29711
TrEMBL
-