ID COX1_TETPY Reviewed; 698 AA.
AC P11947;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-APR-2013, entry version 83.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=1.9.3.1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=COI;
OS Tetrahymena pyriformis.
OG Mitochondrion.
OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5908;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ST;
RX PubMed=2833363; DOI=10.1007/BF00405758;
RA Ziaie Z., Suyama Y.;
RT "The cytochrome oxidase subunit I gene of Tetrahymena: a 57 amino acid
RT NH2-terminal extension and a 108 amino acid insert.";
RL Curr. Genet. 12:357-368(1987).
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; L28677; AAA32102.2; -; Genomic_DNA.
DR EMBL; X06133; CAB57808.1; -; Genomic_DNA.
DR PIR; S00742; S00742.
DR ProteinModelPortal; P11947; -.
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; -; 2.
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; 2.
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 1 698 Cytochrome c oxidase subunit 1.
FT /FTId=PRO_0000183425.
FT TRANSMEM 65 85 Helical; (Potential).
FT TRANSMEM 113 133 Helical; (Potential).
FT TRANSMEM 147 167 Helical; (Potential).
FT TRANSMEM 304 324 Helical; (Potential).
FT TRANSMEM 349 369 Helical; (Potential).
FT TRANSMEM 395 415 Helical; (Potential).
FT TRANSMEM 434 454 Helical; (Potential).
FT TRANSMEM 468 488 Helical; (Potential).
FT TRANSMEM 498 518 Helical; (Potential).
FT TRANSMEM 533 553 Helical; (Potential).
FT TRANSMEM 574 594 Helical; (Potential).
FT TRANSMEM 613 633 Helical; (Potential).
FT METAL 111 111 Iron (heme A axial ligand) (Probable).
FT METAL 401 401 Copper B (Probable).
FT METAL 405 405 Copper B (Probable).
FT METAL 450 450 Copper B (Probable).
FT METAL 451 451 Copper B (Probable).
FT METAL 536 536 Iron (heme A3 axial ligand) (Probable).
FT METAL 538 538 Iron (heme A axial ligand) (Probable).
FT CROSSLNK 401 405 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
SQ SEQUENCE 698 AA; 81747 MW; D6B0F488A3109A72 CRC64;
MLYIFNSFDN MWVDFIEQTK SFKVSVNNYF YYLNKIKKLF TYLNDLRKHI LKKYVYTINH
KRIAINYLYF SMVTGLSGAA LATMIRMELA HPESPFFKGD SLRYLQVVTA HGLIMVFFVV
VPILFGGFAN FLIPYHVGSK DVAYPRLNSI GFWIQPCGYI LLAKIGFLRP QFWRYYDKTS
FSFPFLEKMK YNQYKEYKND YLFYLDFLKK EITDDHSFFW KARKVIKLPQ YSVFSFVPLK
LMMWKTMINY PESFWYAASR VVQSRRKKVF VTKCSARTLT TAGWTFITPF SSNIKYTGVG
SQDILILSVV FAGISTTISF TNLLITRRTL AMPGMRHRRV LMPFVTISIF LTLRMLATIT
PVLGAAVIMM AFDRHWQTTF FEYAYGGDPI LSQHLFWFFG HPEVYVLIIP TFGFINMIVP
HNNTRRVASK HHMIWAIYVM AYMGYLVWGH HMYLVGLDHR SRTMYSTITI MISMPATIKV
VNWTLSLVNG ALKVDLPFLF SMSFLLLFLV AGFTGMWLSH VSLNVSMHDT FYVVAHFHIM
LSGAAITGIF SGFYYYFNAL FGIKFSRMFG YMHLIYYSGG QWVAFVPQFY LGFSGMPRRI
HDYPVVFMGW HSMSTAGHFI TLIGIMFFFL MIFDSHIERR AATSSTLGLP RWYKRISYYI
FKIRYLQHNK AKMNGIPGST VRLMLIDRHF AEFEVFKK
//
