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Information on EC 1.16.3.1 - ferroxidase and Organism(s) Mycobacterium tuberculosis and UniProt Accession I6WZK7

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     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.3 With oxygen as acceptor
                1.16.3.1 ferroxidase
IUBMB Comments
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: I6WZK7
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
ferritin, ceruloplasmin, ferroxidase, apoferritin, xanthine oxidoreductase, caeruloplasmin, l-ferritin, hephaestin, bacterioferritin, hp-nap, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multicopper oxidase
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mycobacterial multicopper oxidase
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bacterioferritin B
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caeruloplasmin
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ceruloplasmin
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ferro:O2 oxidoreductase
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ferroxidase I
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ferroxidase, iron II:oxygen oxidoreductase
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iron(II): oxygen oxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
Fe(II):oxygen oxidoreductase
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-37-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
show the reaction diagram
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?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
show the reaction diagram
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-
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
four copper ions are coordinated in two centers comprise the multicopper oxidase active site
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
membrane associated probably by lipidation after export across the inner membrane by the twin-arginine translocation system
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold
physiological function
multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 56000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determined at 3 A. The crystallographic data implicate the importance of the extended C-terminal region in the iron entry from the three-fold channels to the ferroxidase centre and making iron more readily accessible for the oxidation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C35A
putative lipidation site is dispensable for MmcO activity: mutation shows only minor impact on enzymatic activity
C486A
cysteine 486 is required for MmcO activity. Mutation results in inactive Rv0846c protein which does not protect Mycobacterium tuberculosis against copper stress
additional information
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a truncated protein (having 1-167 amino acids, molecular weight ,18 kDa) is generated: The truncated protein shows a 3.5fold reduction in the oxidation rate of Fe(II). Lack of C-terminus has an impact of the stability of the protein. Truncated BfrB starts unfolding on exposure to even a very low temperature of 30°C whereas the native protein remains almost unaffected till 50°C before denaturing rapidly
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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truncated BfrB starts unfolding on exposure to even a very low temperature of 30°C whereas the native protein remains almost unaffected till 50°C before denaturing rapidly
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using NH4SO4 precipitation and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the mmcO gene is increased by copper
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khare, G.; Gupta, V.; Nangpal, P.; Gupta, R.; Sauter, N.; Tyagi, A.
Ferritin structure from Mycobacterium tuberculosis: Comparative study with homologues identifies extended C-terminus involved in ferroxidase activity
PLoS ONE
6
e18570
2011
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Rowland, J.L.; Niederweis, M.
A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
J. Bacteriol.
195
3724-3373
2013
Mycobacterium tuberculosis (I6WZK7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (I6WZK7)
Manually annotated by BRENDA team