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 03-APR-2013, entry version 82.
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.
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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 to 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:EC.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR000883; Cyt_c_Oxase_su1.
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; COX1; 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; (Potential).
FT TRANSMEM 58 78 Helical; (Potential).
FT TRANSMEM 104 124 Helical; (Potential).
FT TRANSMEM 147 167 Helical; (Potential).
FT TRANSMEM 184 204 Helical; (Potential).
FT TRANSMEM 236 256 Helical; (Potential).
FT TRANSMEM 268 288 Helical; (Potential).
FT TRANSMEM 311 331 Helical; (Potential).
FT TRANSMEM 339 359 Helical; (Potential).
FT TRANSMEM 373 393 Helical; (Potential).
FT TRANSMEM 413 433 Helical; (Potential).
FT TRANSMEM 453 473 Helical; (Potential).
FT METAL 63 63 Iron (heme A axial ligand) (Probable).
FT METAL 242 242 Copper B (Probable).
FT METAL 246 246 Copper B (Probable).
FT METAL 291 291 Copper B (Probable).
FT METAL 292 292 Copper B (Probable).
FT METAL 377 377 Iron (heme A3 axial ligand) (Probable).
FT METAL 379 379 Iron (heme A axial ligand) (Probable).
FT CROSSLNK 242 246 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
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
//
