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Database: UniProt
Entry: A0A1D8GA71_9ACTN
LinkDB: A0A1D8GA71_9ACTN
Original site: A0A1D8GA71_9ACTN 
ID   A0A1D8GA71_9ACTN        Unreviewed;       571 AA.
AC   A0A1D8GA71;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   Name=ctaD_4 {ECO:0000313|EMBL:AOT62355.1};
GN   ORFNames=A4G23_05251 {ECO:0000313|EMBL:AOT62355.1};
OS   Streptomyces rubrolavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT62355.1, ECO:0000313|Proteomes:UP000095349};
RN   [1] {ECO:0000313|EMBL:AOT62355.1, ECO:0000313|Proteomes:UP000095349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJM4426 {ECO:0000313|EMBL:AOT62355.1,
RC   ECO:0000313|Proteomes:UP000095349};
RA   Kim J.-G.;
RT   "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) 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; CP017316; AOT62355.1; -; Genomic_DNA.
DR   RefSeq; WP_069979144.1; NZ_CP017316.1.
DR   AlphaFoldDB; A0A1D8GA71; -.
DR   STRING; 285473.A4G23_05251; -.
DR   KEGG; srn:A4G23_05251; -.
DR   PATRIC; fig|285473.5.peg.5534; -.
DR   OrthoDB; 9803294at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000095349; Chromosome.
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   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   Oxidoreductase {ECO:0000313|EMBL:AOT62355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095349};
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        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        163..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        201..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        247..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        393..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        465..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          24..530
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   571 AA;  63486 MW;  16A0A00DAFC88575 CRC64;
     MATTTEPPAP VPARRRAGRV VVDWLTTTDH KKIGHLYLIT SFAFFLVGGA LALLLRAELA
     RPGLQLISNE QYNQAFTLHG TVMLLLFATP TFTGFANAIM PLQIGAPDVA FPRLNMLSYW
     LFLFGSLIVL ASLLQPQGTA DFGWTAYTPL SLEERSPSPG SDMWIMGLAL TGFGTILGSV
     NFITTIVCMR APGMTMFRMP IFTWNVLLTS ILVLMAFPVL AAALLALESD RVFGSTVFAP
     ENGGALLWQH LFWFFGHPEV YILALPFFGV VSEILPVFCR KPLFGYVGLV GATIAIAGLS
     IMVWAHHMFA TGAVLLPFFS FMTFLIAVPT GVKFFNWAGT MWNGSITFET PMLWSVGFLV
     TFLFGGLTGV VLGSPPMDWH VTDTYFVVAH FHYVLFGTIV FAMFAGFHFW WPKMTGTMLD
     ERLGRIHFWT LFVGFHLTFL VQHWLGAEGM PRRYADYLAA DGFTWLNMLS SIGAFLLGLS
     TLPFLYNVWK TAKAGKRVGV DDPWGYGRSL EWVTSCPPPR HNFVTLPRVR SESPAFDLHH
     PDMAAVDRGW NKGRDVVDPD NATVVTRDDD R
//
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