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P80440 (COX1_ALLMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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
OrganismAllomyces macrogynus
Taxonomic identifier28583 [NCBI]
Taxonomic lineageEukaryotaFungiBlastocladiomycotaBlastocladiomycetesBlastocladialesBlastocladiaceaeAllomyces

Protein attributes

Sequence length536 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 – 536536Cytochrome c oxidase subunit 1
PRO_0000183279

Regions

Transmembrane21 – 4121Helical; Potential
Transmembrane62 – 8221Helical; Potential
Transmembrane105 – 12521Helical; Potential
Transmembrane151 – 17121Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane240 – 26021Helical; Potential
Transmembrane272 – 29221Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane343 – 36321Helical; Potential
Transmembrane382 – 40221Helical; Potential
Transmembrane417 – 43721Helical; Potential
Transmembrane461 – 48121Helical; Potential

Sites

Metal binding671Iron (heme A axial ligand) Probable
Metal binding2461Copper B Probable
Metal binding2501Copper B Probable
Metal binding2951Copper B Probable
Metal binding2961Copper B Probable
Metal binding3811Iron (heme A3 axial ligand) Probable
Metal binding3831Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link246 ↔ 2501'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P80440 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7DE8DF291EAE4091

FASTA53659,445
        10         20         30         40         50         60 
MFQRNTVYRW LFSTNAKDIG TLYLVFSIFA GMIGTAFSVL IRFELAGPGV QYLYGDHQLY 

        70         80         90        100        110        120 
NVIITAHAFI MIFFLVMPAM LGGFGNYFVP IMIGAPDMAF PRLNNISFWL LPPSLILLVG 

       130        140        150        160        170        180 
SAFVEQGAGT GWTVYPPLSS IGFHSGGSVD LAIFSLHLAG ISSMLGSINF ITTILNMRAP 

       190        200        210        220        230        240 
GMTMHKLPLF VWSILITAIL LLLSLPVLAG AITMLLTDRN LNTTFYDPAG GGDPVLYQHL 

       250        260        270        280        290        300 
FWFFGHPEVY IIIIPGFGII SQVISTFSRK PIFGYLGMVY AMASIGILGF IVWSHHMYTV 

       310        320        330        340        350        360 
GLDVDTRAYF TAATMIIAVP TGIKIFSWLA TLYGGNILYR TPAYFALGFL FLFTIGGVTG 

       370        380        390        400        410        420 
VMLANASLDV ALHDTYYVVA HFHYVLSMGA VFALFAGFYY WIGKITGKQY NEFWGQVHFW 

       430        440        450        460        470        480 
TMFIGVNVTF FPMHFLGLNG MPRRIPDYPD AFTQWNVISS FGSIISIVST IVFLYGLYLT 

       490        500        510        520        530 
LSQPAVSLAN NYWHVPSFFS STHSLYGDTT QTSSSLEWVL PSPPAFHAFN HLPVQS 

« Hide

References

[1]"Molecular phylogeny of Allomyces macrogynus: congruency between nuclear ribosomal RNA- and mitochondrial protein-based trees."
Paquin B., Forget L., Roewer I., Lang B.F.
J. Mol. Evol. 41:657-665(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46923 / Burma 3-35 (35OC).
[2]"The mitochondrial DNA of Allomyces macrogynus: the complete genomic sequence from an ancestral fungus."
Paquin B., Lang B.F.
J. Mol. Biol. 255:688-701(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46923 / Burma 3-35 (35OC).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41288 Genomic DNA. Translation: AAC49234.1.
PIRS63651.
RefSeqNP_043733.1. NC_001715.1.

3D structure databases

ProteinModelPortalP80440.
SMRP80440. Positions 7-529.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID801856.

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_ALLMA
AccessionPrimary (citable) accession number: P80440
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 86 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