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Database: UniProt/SWISS-PROT
Entry: COX1A_STRCO
LinkDB: COX1A_STRCO
Original site: COX1A_STRCO 
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
//
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