ID COX1_LEITA Reviewed; 549 AA.
AC P14544;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-APR-2013, entry version 77.
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 Leishmania tarentolae (Sauroleishmania tarentolae).
OG Mitochondrion.
OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC Leishmaniinae; Leishmania; lizard Leishmania.
OX NCBI_TaxID=5689;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6096360;
RA de la Cruz V.F., Neckelmann N., Simpson L.;
RT "Sequences of six genes and several open reading frames in the
RT kinetoplast maxicircle DNA of Leishmania tarentolae.";
RL J. Biol. Chem. 259:15136-15147(1984).
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 PIR; D30010; D30010.
DR ProteinModelPortal; P14544; -.
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 1 549 Cytochrome c oxidase subunit 1.
FT /FTId=PRO_0000183350.
FT TRANSMEM 18 38 Helical; (Potential).
FT TRANSMEM 42 62 Helical; (Potential).
FT TRANSMEM 66 86 Helical; (Potential).
FT TRANSMEM 100 120 Helical; (Potential).
FT TRANSMEM 148 168 Helical; (Potential).
FT TRANSMEM 186 206 Helical; (Potential).
FT TRANSMEM 222 242 Helical; (Potential).
FT TRANSMEM 246 266 Helical; (Potential).
FT TRANSMEM 269 289 Helical; (Potential).
FT TRANSMEM 306 326 Helical; (Potential).
FT TRANSMEM 340 360 Helical; (Potential).
FT TRANSMEM 379 399 Helical; (Potential).
FT TRANSMEM 402 422 Helical; (Potential).
FT TRANSMEM 460 480 Helical; (Potential).
FT TRANSMEM 484 504 Helical; (Potential).
FT TRANSMEM 520 540 Helical; (Potential).
FT METAL 64 64 Iron (heme A axial ligand) (Probable).
FT METAL 243 243 Copper B (Probable).
FT METAL 247 247 Copper B (Probable).
FT METAL 292 292 Copper B (Probable).
FT METAL 293 293 Copper B (Probable).
FT METAL 378 378 Iron (heme A3 axial ligand) (Probable).
FT METAL 380 380 Iron (heme A axial ligand) (Probable).
FT CROSSLNK 243 247 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
SQ SEQUENCE 549 AA; 63272 MW; F6DD04815A4917C2 CRC64;
MFWLCLVCLS VSHKMIGLCY LLVAILSGFV GYVYSLFIRL ELSLIGCGIL FGDYQFYNVL
ITSHGLIMVF AFIMPVMMGG LVNYFIPVMA GFPDMVFPRL NNMSFWMYLA GFGCVVNGFL
TEEGMGVGWT LYPTLICIDF HSSLACDFVM FAVHLLGISS ILNSINLLGT LFCCRRKFFS
FLSWSLFIWA ALITAILLII TLPVLAGGVT LILCDRNFNT SFYDVVGGGD LILFQHIFWF
FGHPEVYIIL LPVFGLISTI VEVIGFRCVF STVAMIYSMI LIAILGMFVW AHHMFVVGMD
VDSRAYFGGV SILIGLPTCV KLFNWIYSFL YTDMIITFEV YFVIMFIFMF LIGAVTGLFL
SNVGIDIMLH DTYFVVGHFH YVLSLGAVVG FFTGFIHFLA KWLPIELYLF WMFYFISTLF
IGSNMLFFPM HSLGMYAFPR RISDYPVSFL FWSSFMLYGM LLLASLILFL CALFCVFLFW
DYCLFFVSLF VFSLYCFFYF STWLPCVMVL YLLLVDFAHI VLDYLFLILC FCFVFFIFFW
QSLFLFFYI
//
