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Database: UniProt
Entry: A0A1Z4BTJ2_9GAMM
LinkDB: A0A1Z4BTJ2_9GAMM
Original site: A0A1Z4BTJ2_9GAMM 
ID   A0A1Z4BTJ2_9GAMM        Unreviewed;       543 AA.
AC   A0A1Z4BTJ2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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 {ECO:0000313|EMBL:ASF44588.1};
GN   ORFNames=AADEFJLK_01338 {ECO:0000313|EMBL:POZ52731.1}, CEK71_00065
GN   {ECO:0000313|EMBL:ASF44588.1};
OS   Methylovulum psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylovulum.
OX   NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF44588.1, ECO:0000313|Proteomes:UP000197019};
RN   [1] {ECO:0000313|EMBL:ASF44588.1, ECO:0000313|Proteomes:UP000197019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF44588.1,
RC   ECO:0000313|Proteomes:UP000197019};
RA   Mateos-Rivera A.;
RT   "Genome Sequencing of the methanotroph Methylovulum psychrotolerants str.
RT   HV10-M2 isolated from a high-altitude environment.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:POZ52731.1, ECO:0000313|Proteomes:UP000237423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sph1 {ECO:0000313|EMBL:POZ52731.1,
RC   ECO:0000313|Proteomes:UP000237423};
RA   Oshkin I.Y., Miroshnikov K., Belova S.E., Korzhenkov A., Toshchakov S.V.,
RA   Dedysh S.N.;
RT   "Draft Genome Sequence of Methylobacter psychrotolerans Sph1T, an Obligate
RT   Methanotroph from Low-Temperature Environments.";
RL   Submitted (NOV-2017) 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|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; CP022129; ASF44588.1; -; Genomic_DNA.
DR   EMBL; PGFZ01000002; POZ52731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4BTJ2; -.
DR   KEGG; mpsy:CEK71_00065; -.
DR   OrthoDB; 9803294at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000197019; Chromosome.
DR   Proteomes; UP000237423; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
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; cd01663; Cyt_c_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; IPR033944; Cyt_c_oxase_su1_dom.
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:UP000197019};
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        43..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        84..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        126..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        167..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        205..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        295..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        358..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        394..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        430..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        471..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          25..538
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   543 AA;  60779 MW;  7EB1A178DFEE5F24 CRC64;
     MSAVVAEHDE HHDEHHHDDH AHGPEKGLLR WIVTTNHKDI GTLYLLFALA MFFVGGVMAL
     VIRAELFEPG LQFVEPQFFN SMTTMHALVM VFGAVMPGFV GLANWMIPMM IGAPDMALPR
     MNNMSFWMLV AGVLLLATTL FMEGGAPAAG WTLYPPLVLQ TGKALPFAIF SVHLLGISSI
     MGAINIIATI FNMRAPAMTL MKMPLFVWTW LITAFLLIAV MPVFAGAVTM LLTDRFFETS
     FFDAAGGGDP VLYQHIFWFF GHPEVYIMIL PTFGVASTII PVFARKPLFG YSSMVYATAS
     IAFLSFIVWA HHMFTVGMPI AGELYFMYAT MLIAIPTGVK VFNWTATMWK GSMTFETPML
     FSIAFVVLFT MGGFTGLMMS IAPSDFQYHD TYFIVAHFHY VLVPSSIFIL MAAGYYWLPK
     WTGHMYNEKI GQLHFWLSVV SVNILFFPQH FLGLAGMPRR IPDYAVQFAD WNMISSIGGF
     IFGISQLLFL YIVIDTIRGG TGEKVSDEVW EDAHKHGLEW TLPSPAPYHT FTTPPTVIPT
     EHI
//
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