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Database: UniProt
Entry: A0A1H1TK37_9ACTN
LinkDB: A0A1H1TK37_9ACTN
Original site: A0A1H1TK37_9ACTN 
ID   A0A1H1TK37_9ACTN        Unreviewed;       652 AA.
AC   A0A1H1TK37;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   ORFNames=SAMN04489717_3232 {ECO:0000313|EMBL:SDS60562.1};
OS   Actinopolymorpha singaporensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Actinopolymorphaceae; Actinopolymorpha.
OX   NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS60562.1, ECO:0000313|Proteomes:UP000198983};
RN   [1] {ECO:0000313|EMBL:SDS60562.1, ECO:0000313|Proteomes:UP000198983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS60562.1,
RC   ECO:0000313|Proteomes:UP000198983};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT629732; SDS60562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1TK37; -.
DR   STRING; 117157.SAMN04489717_3232; -.
DR   OrthoDB; 9803294at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000198983; Chromosome i.
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   Reference proteome {ECO:0000313|Proteomes:UP000198983};
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        60..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        98..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        185..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        221..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        283..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        341..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        377..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        412..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        448..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        493..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        612..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          32..553
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   652 AA;  72328 MW;  E90E1A6F14CA5D9E CRC64;
     MATADTTAGS TATGALTGTL PERAVAEDAV GGKLRKVWAE EPGFIGFLST VNHKRIGRRY
     LVTAAFFFLL AGIQAMIMRT QLGTPENRLV DPALYNQLFS LHGTAMIFFF ATPMNSGFGN
     LFLPLMVGTR DMAFPRLNAL SYWIFLFSGL FMFVSLPLGL APNGGWFAYV PLTTSEYLPG
     LHLDFYTLGL LFLAISTTVG SINLIVTALK MRAPGMSLNR VPVFVWAVVT QSFMLIFALP
     PLDLANGMLF SDRRFGTHFF DPAKGGDTIL WQHLFWLFGH PDVYIIVLPA MGIISSVIPT
     FSRRPIAAYP LVVIATVATG IISFGVWVHH MFAVGLSQVS LSFFSAATLT ISLPAGIQMF
     AWLATMWRGR VVLTTPMLYA IGFIVTFVLG GVTGVMFAVV PFDQQVTDSY FVVAHFHYVL
     FGGAVMPMLA GWFYWWPKFT GRMTHRKASI WSFVWVFVGF NLTFFPMHIA GLLGMPRRIY
     TYEPGLGWTP YNLVSTIGGY VLAVGFLLTL GVLLHSYLRG EKAPDDPWGS NTLEWATSSP
     PQPYNFPVIP TVHSLDPLWD NQTLRSMEEL RHDDQRTMTE KHETLRTTEL DARFEGVMPM
     PSDTAIPILV ALLLTATVVL LLLAFYIGAV VAFGAMLLVV AWWLWHRPGV EE
//
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