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P98053 (COXM_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alternative cytochrome c oxidase subunit 2

EC=1.9.3.1
Alternative name(s):
Alternative cytochrome c oxidase polypeptide II
Cytochrome BB3 subunit 2
Oxidase BB(3) subunit 2
Gene names
Name:coxM
Ordered Locus Names:bll3785
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Developmental stage

Bacteroid (nitrogen-fixing endosymbiont).

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandCopper
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

cytochrome-c oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Alternative cytochrome c oxidase subunit 2
PRO_0000183724

Regions

Topological domain1 – 4040Periplasmic Potential
Transmembrane41 – 6121Helical; Potential
Topological domain62 – 8322Cytoplasmic Potential
Transmembrane84 – 10421Helical; Potential
Topological domain105 – 277173Periplasmic Potential

Sites

Metal binding1901Copper A Probable
Metal binding2251Copper A Probable
Metal binding2291Copper A Probable
Metal binding2331Copper A Probable

Sequences

Sequence LengthMass (Da)Tools
P98053 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D262ADE2233D36E1

FASTA27731,327
        10         20         30         40         50         60 
MAVALILLLI AIGSVLFHLF SPWWWTPIAT NWGYIDDTIN ITFWITGFVF TAVILFMAYC 

        70         80         90        100        110        120 
VFRFHHKEGR QAAYNPENKK LEWWLSVGTG VGVAAMLAPG LVVWHQFVTV PADATEVEIM 

       130        140        150        160        170        180 
GQQWQWSFRL PGKDGRLGTS DVRNISPENP MGLNRDDPHG QDDVVIENGD LHLPIGKPVK 

       190        200        210        220        230        240 
VLLRSVDVLH DFYVPEFRAK MDMVPGMVTY FWIRPIRTGT FDVLCAELCG AAHYQMRAKV 

       250        260        270 
IVEAESDYHA WLEQQKTFAG LSGRNAVVRA KYNSGDD 

« Hide

References

« Hide 'large scale' references
[1]"Genes for a second terminal oxidase in Bradyrhizobium japonicum."
Bott M., Preisig O., Hennecke H.
Arch. Microbiol. 158:335-343(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110spc4.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68547 Genomic DNA. Translation: CAA48547.1.
BA000040 Genomic DNA. Translation: BAC49050.1.
PIRB48364.
RefSeqNP_770425.1. NC_004463.1.

3D structure databases

ProteinModelPortalP98053.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.bll3785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC49050; BAC49050; BAC49050.
GeneID1053041.
KEGGbja:bll3785.
PATRIC21191037. VBIBraJap65052_3776.

Phylogenomic databases

eggNOGCOG1622.
HOGENOMHOG000268576.
KOK02275.
OMARAKMDMI.
OrthoDBEOG68SVXT.
ProtClustDBCLSK2747381.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-3809-MONOMER.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOXM_BRADU
AccessionPrimary (citable) accession number: P98053
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families