ID D9XV14_9ACTN Unreviewed; 577 AA.
AC D9XV14;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN ORFNames=SSRG_00529 {ECO:0000313|EMBL:EFL37725.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL37725.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL37725.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL37725.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. CO I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme A of subunit
CC 1 to the bimetallic center formed by heme A3 and copper B.
CC {ECO:0000256|ARBA:ARBA00025218, ECO:0000256|RuleBase:RU363061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00029368,
CC ECO:0000256|RuleBase:RU363061};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU000370}.
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DR EMBL; GG657758; EFL37725.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XV14; -.
DR STRING; 467200.SSRG_00529; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_11; -.
DR OrthoDB; 9803294at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002968; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU363061};
KW Copper {ECO:0000256|RuleBase:RU363061};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU363061};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW Metal-binding {ECO:0000256|RuleBase:RU363061};
KW Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000370};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 165..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 203..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 387..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 467..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 26..532
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT REGION 537..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64014 MW; 17F0E701DED246CC CRC64;
MTAVDQPIRT TTEPPPRKPG NVVVAWLTST DHKTIGSLYM ITSFAFFLIG GVMALVIRAE
LARPGLQIVS NEQFNQSFTM HGTVMLLMFA TPLFAGFANW IMPLQIGAPD VAFPRLNMFA
YWLFLFGSLI ALGGFLTPNG AADFGWFAYS PLTDAEHSPN IGSDLWIMGL GFSGFGTILG
SVNFITTIIC MRAPGMTMFR MPIFTWNVLL TGVLVLLAFP VLAAALFALE ADRKFGAHVF
DAANGGALLW QHLFWFFGHP EVYIIALPFF GIISEIIPVF SRKPIFGYMG LIGATITIAG
LSVTVWAHHM FVTGGVLLPF FSFMSFLIAI PTGVKFFNWT GTMWKGSLSF ETPMLWSAGF
LVTFLFGGLT GVLLASPPLD FHVSDSYFVV AHFHYVVFGT VVFAMFAGFY FWWPKFTGKM
LDERLGKIHF WTLFVGFHGT FLVQHWLGAE GMPRRYADYL ASDGFTALNT ASSIGSFLLG
LSMLPFLYNI WKTAKYGRPV GVDDPWGYGR SLEWATACPP PRHNFVTLPR IRSESPTFDL
RHPGLSRIDQ EENAGRRDAV EPEPHGRAHR PPLDGSE
//
