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Q0H8Y4 (COX1_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:COX1
Encoded onMitochondrion
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

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

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Cytochrome c oxidase subunit 1
PRO_0000271141

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane99 – 11921Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane266 – 28621Helical; Potential
Transmembrane304 – 32421Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane372 – 39221Helical; Potential
Transmembrane413 – 43321Helical; Potential
Transmembrane455 – 47521Helical; Potential

Sites

Metal binding611Iron (heme A axial ligand) By similarity
Metal binding2401Copper B By similarity
Metal binding2441Copper B By similarity
Metal binding2891Copper B By similarity
Metal binding2901Copper B By similarity
Metal binding3751Iron (heme A3 axial ligand) By similarity
Metal binding3771Iron (heme A axial ligand) By similarity

Amino acid modifications

Lipidation3181N6-myristoyl lysine By similarity
Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0H8Y4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 7381FC2EB2788C66

FASTA52857,899
        10         20         30         40         50         60 
MVRWLYSTNA KDIGTLYLIF AVFAAMIGTA FSVLIRMELA APGVQYLNGD HQLYNVIITA 

        70         80         90        100        110        120 
HAFVMIFFMV MPAMVGGFGN YLVPVMIGAP DMAFPRLNNI SFWLLPPSLI LLLASAFVEQ 

       130        140        150        160        170        180 
GAGTGWTVYP PLSGLQSHSG GSVDLAIFSL HLSGISSMLG AMNFITTVLN MRNPGMTLHK 

       190        200        210        220        230        240 
LPLFVWAIFV TAILLLLSLP VLAGAITMLL TDRNFNTSFY DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILIIPG FGMVSHIVSA FSGKPVFGYL GMVYAMFSIG ILGFLVWSHH MYAVGLDVDT 

       310        320        330        340        350        360 
RAYFTAATMI IAVPTGIKIF SWLATLYGGS LRITTPMLFA LGFIALFTIG GLTGVILANA 

       370        380        390        400        410        420 
SLDVALHDTY YVVAHFHYVL SMGAVFALFG GFYFWTPKII GKTFNENLGR IHFWTLFVGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLGGMPRRIP DYPDAFAAWN AISSFGSLVS VVATALFGYI IYDILVNGKP 

       490        500        510        520 
VDANPWAVPA FFQSTPEFWM ESHTASSLEW ALESPTPFHS FNMLPVQS 

« Hide

References

[1]"Annotation of mitochondrial genome of Ustilago maydis and comparative analysis of basidiomycete mtDNAs."
Kennell J.C., Boehmer C.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.
[2]"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ157700 Genomic DNA. Translation: AAZ67011.1.
AACP01000277 Genomic DNA. No translation available.
AACP01000278 Genomic DNA. No translation available.
RefSeqYP_762688.1. NC_008368.1.

3D structure databases

ProteinModelPortalQ0H8Y4.
SMRQ0H8Y4. Positions 3-521.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4308276.
KEGGuma:UsmafMp08.

Phylogenomic databases

KOK02256.
OrthoDBEOG72C58S.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_USTMA
AccessionPrimary (citable) accession number: Q0H8Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways