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Database: UniProt
Entry: P48868
LinkDB: P48868
Original site: P48868 
ID   COX1_WICCA              Reviewed;         535 AA.
AC   P48868;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   01-OCT-2014, entry version 89.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=1.9.3.1;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=COX1;
OS   Wickerhamomyces canadensis (Yeast) (Pichia canadensis).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1156965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21;
RX   PubMed=8536312; DOI=10.1007/BF00311880;
RA   Sekito T., Okamoto K., Kitano H., Yoshida K.;
RT   "The complete mitochondrial DNA sequence of Hansenula wingei reveals
RT   new characteristics of yeast mitochondria.";
RL   Curr. Genet. 28:39-53(1995).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; D31785; BAA06563.2; -; Genomic_DNA.
DR   PIR; S58740; S58740.
DR   RefSeq; NP_038208.1; NC_001762.1.
DR   ProteinModelPortal; P48868; -.
DR   SMR; P48868; 1-533.
DR   GeneID; 800565; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR000883; COX1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    535       Cytochrome c oxidase subunit 1.
FT                                /FTId=PRO_0000183341.
FT   TRANSMEM     17     37       Helical. {ECO:0000255}.
FT   TRANSMEM     58     78       Helical. {ECO:0000255}.
FT   TRANSMEM    104    124       Helical. {ECO:0000255}.
FT   TRANSMEM    147    167       Helical. {ECO:0000255}.
FT   TRANSMEM    184    204       Helical. {ECO:0000255}.
FT   TRANSMEM    236    256       Helical. {ECO:0000255}.
FT   TRANSMEM    268    288       Helical. {ECO:0000255}.
FT   TRANSMEM    311    331       Helical. {ECO:0000255}.
FT   TRANSMEM    339    359       Helical. {ECO:0000255}.
FT   TRANSMEM    373    393       Helical. {ECO:0000255}.
FT   TRANSMEM    413    433       Helical. {ECO:0000255}.
FT   TRANSMEM    453    473       Helical. {ECO:0000255}.
FT   METAL        63     63       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   METAL       242    242       Copper B. {ECO:0000305}.
FT   METAL       246    246       Copper B. {ECO:0000305}.
FT   METAL       291    291       Copper B. {ECO:0000305}.
FT   METAL       292    292       Copper B. {ECO:0000305}.
FT   METAL       377    377       Iron (heme A3 axial ligand).
FT                                {ECO:0000305}.
FT   METAL       379    379       Iron (heme A axial ligand).
FT                                {ECO:0000305}.
FT   CROSSLNK    242    246       1'-histidyl-3'-tyrosine (His-Tyr).
FT                                {ECO:0000250}.
SQ   SEQUENCE   535 AA;  59025 MW;  97F7C4EFAD1AD50A CRC64;
     MYIQRWLYST NAKDIAILYF IFAIFSGVIG STMSLIIRLE LAAPGNQILH GNHQLFNVLV
     VGHALLMIFF LVMPGLVGGF GNYMLPLLIG ASDMSFARLN NISFWLLPPA LVCLVASTLI
     ESWAGTGWTI YPPLSGIQAH SSPSVDLGIF AIHLTSISSL LGAINFIATS YNMRTNGMSY
     SKMPLFVWAI IITAVMLLLS LPVLTAGVTM LLMDRNFNTS FFEVAGGGDP VLYQHLFWFF
     GHPEVYILIV PGFGIISHIV STYSKKPVFG EISMVYAMAS IAFLGFLVWS HHMYIVGLDA
     DTRAYFTSST MVIAVPTGIK IFSWLATLYG GSIRLAVPML YAIAFLFLFT IGGLTGVALA
     NASLDVAFHD TYYVVGHFHY VLSMGAIFSL FAGYYYWSPQ ILGLYFNERL AQIQFWLIFV
     GANVIFMPMH FLGLQGMPRR IPDYPDAYAG WNYVSSIGSV IAIISLALFI YIIYDQLING
     LTNKIDNKSV VYSKAPDFVE SNTIFANNSI KSASIEFLLN SPPAIHSFNT PAVQS
//
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