ID COX1A_STRCO Reviewed; 578 AA.
AC Q9X813;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 01-MAY-2013, entry version 85.
DE RecName: Full=Probable cytochrome c oxidase subunit 1-alpha;
DE EC=1.9.3.1;
DE AltName: Full=Cytochrome aa3 subunit 1-alpha;
DE AltName: Full=Cytochrome c oxidase polypeptide I-alpha;
GN Name=ctaD1; OrderedLocusNames=SCO2155; ORFNames=SC6G10.28c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptomycineae; Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O.
CC -!- COFACTOR: Binds 1 copper B per subunit (By similarity).
CC -!- COFACTOR: Binds 2 heme groups per subunit (By similarity).
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Associates with subunits II, III and IV to form
CC cytochrome c oxidase (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR EMBL; AL939111; CAB39882.1; -; Genomic_DNA.
DR PIR; T35537; T35537.
DR RefSeq; NP_626411.1; NC_003888.3.
DR ProteinModelPortal; Q9X813; -.
DR STRING; 100226.SCO2155; -.
DR EnsemblBacteria; CAB39882; CAB39882; CAB39882.
DR GeneID; 1097589; -.
DR KEGG; sco:SCO2155; -.
DR PATRIC; 23733962; VBIStrCoe124346_2190.
DR eggNOG; COG0843; -.
DR HOGENOM; HOG000085274; -.
DR KO; K02274; -.
DR OMA; FLIGGIM; -.
DR ProtClustDB; CLSK2519270; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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 InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; COX1; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane; Complete proteome; Copper; Electron transport; Heme;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 578 Probable cytochrome c oxidase subunit 1-
FT alpha.
FT /FTId=PRO_0000183452.
FT TRANSMEM 44 64 Helical; (Potential).
FT TRANSMEM 93 113 Helical; (Potential).
FT TRANSMEM 125 145 Helical; (Potential).
FT TRANSMEM 174 194 Helical; (Potential).
FT TRANSMEM 217 237 Helical; (Potential).
FT TRANSMEM 262 282 Helical; (Potential).
FT TRANSMEM 294 314 Helical; (Potential).
FT TRANSMEM 319 339 Helical; (Potential).
FT TRANSMEM 363 383 Helical; (Potential).
FT TRANSMEM 402 422 Helical; (Potential).
FT TRANSMEM 437 457 Helical; (Potential).
FT TRANSMEM 480 500 Helical; (Potential).
FT METAL 90 90 Iron (heme A axial ligand) (By
FT similarity).
FT METAL 268 268 Copper B (By similarity).
FT METAL 272 272 Copper B (By similarity).
FT METAL 317 317 Copper B (By similarity).
FT METAL 318 318 Copper B (By similarity).
FT METAL 401 401 Iron (heme A3 axial ligand) (By
FT similarity).
FT METAL 403 403 Iron (heme A axial ligand) (By
FT similarity).
FT CROSSLNK 268 272 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
SQ SEQUENCE 578 AA; 64122 MW; 2A25FF2A913DC461 CRC64;
MSILNEPQGA SAAEDSYENE LPVRRKQPGN VVIKWLTTTD HKTIGTMYLV TSFAFFVIGG
VMALFMRAEL ARPGLQIMSN EQFNQAFTMH GTIMLLMFAT PLFAGFANWI MPLQIGAPDV
AFPRLNMFAY WLYLFGSTIA VGGFLTPQGA ADFGWFAYSP LSDAVHSPGI GGDLWIMGLA
FSGFGTILGS VNFITTIICM RAPGMTMFRM PIFTWNVLLT GVLVLLAFPV LAAALFALEA
DRKFGAHIFD SSNGGALLWQ HLFWFFGHPE VYIIALPFFG IVSEIIPVFS RKPIFGYMGL
IGATIAIAGL SVTVWAHHMY VTGGVLLPFF SFMTFLIAVP TGVKFFNWIG TMWKGSLSFE
TPMLWSTGFL ITFLFGGLTG VILASPPLDF HVSDSYFVVA HFHYVVFGTV VFAMFAGFHF
WWPKFTGKML DERLGKITFW TLFVGFHGTF LVQHWLGAEG MPRRYADYLA ADGFTALNTI
STISSFLLGM SILPFFYNIW KTAKYGKKIE VDDPWGYGRS LEWATSCPPP RHNFLTLPRI
RSESPAFDLH HPEISAIDQL ENVGHGEKAL AGGKEAGK
//