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P48866 (COX1_CHOCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismChondrus crispus (Carragheen moss) (Irish moss)
Taxonomic identifier2769 [NCBI]
Taxonomic lineageEukaryota › Rhodophyta › Florideophyceae › Gigartinales › Gigartinaceae › Chondrus

Protein attributes

Sequence length532 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 – 532532Cytochrome c oxidase subunit 1
PRO_0000183313

Regions

Transmembrane23 – 4321Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane110 – 13021Helical; Potential
Transmembrane153 – 17321Helical; Potential
Transmembrane191 – 21121Helical; Potential
Transmembrane242 – 26221Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane315 – 33521Helical; Potential
Transmembrane345 – 36521Helical; Potential
Transmembrane384 – 40421Helical; Potential
Transmembrane421 – 44121Helical; Potential
Transmembrane463 – 48321Helical; Potential

Sites

Metal binding691Iron (heme A axial ligand) Probable
Metal binding2481Copper B Probable
Metal binding2521Copper B Probable
Metal binding2971Copper B Probable
Metal binding2981Copper B Probable
Metal binding3831Iron (heme A3 axial ligand) Probable
Metal binding3851Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link248 ↔ 2521'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P48866 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A0F18B4B35BA636F

FASTA53259,291
        10         20         30         40         50         60 
MQSFFTQWIS RWIFSTNHKD IGTLYLIFGA FSGVLGGCMS MLIRMELAQP SNHLLLGNHQ 

        70         80         90        100        110        120 
IYNVLITAHA FLMIFFMVMP VMIGGFGNWL VPIMIGSPDM AFPRLNNISF WLLPPSLCLL 

       130        140        150        160        170        180 
LMSALVEVGV GTGWTVYPPL SSIQSHSGGA VDLAIFSLHI SGASSILGAV NFISTILNMR 

       190        200        210        220        230        240 
SPGQSMYRIP LFVWSILVTA FLLLLAVPVL AGAITMLLTD RNFNTSFFDA SGGGDPILYQ 

       250        260        270        280        290        300 
HLFWFFGHPE VYILILPGFG MISHIVSTFS RKPVFGYIGM VYAMVSIGVL GFIVWAHHMY 

       310        320        330        340        350        360 
TVGLDVDTRA YFTAATMIIA VPTGIKIFSW IATIWEGSIH LKTPMLFAIG FIFLFTIGGL 

       370        380        390        400        410        420 
TGIVLANSGL DISLHDTYYV VAHFHYVLSM GAVFAIFAGF YYWFGKITGL QYPETLGQIH 

       430        440        450        460        470        480 
FWSTFIGVNL TFMPMHFLGL AGMPRRIPDY PDAYAGWNLI ASYGSYIALF STLFFFYIVF 

       490        500        510        520        530 
VSLTSNNPCT NFPWEFNKSK TYGVSTLEWI VTSPPAYHTF EEMPLIYETK SN

« Hide

References

[1]"Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus (Gigartinales). Gene content and genome organization."
Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M., Kloareg B.
J. Mol. Biol. 250:484-495(1995) [PubMed: 7616569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Apices.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z47547 Genomic DNA. Translation: CAA87603.1.
PIRS59087.
RefSeqNP_062482.1. NC_001677.2.

3D structure databases

ProteinModelPortalP48866.
SMRP48866. Positions 8-522.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID809360.

Family and domain databases

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]
Gene3DG3DSA:1.20.210.10. COX1. 1 hit.
PANTHERPTHR10422. COX1. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. COX1. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_CHOCR
AccessionPrimary (citable) accession number: P48866
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 31, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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