ID I4N7X6_9PSED Unreviewed; 530 AA.
AC I4N7X6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN ORFNames=PMM47T1_07266 {ECO:0000313|EMBL:EIK97566.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK97566.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK97566.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK97566.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIK97566.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJWX01000004; EIK97566.1; -; Genomic_DNA.
DR RefSeq; WP_008367199.1; NZ_AJWX01000004.1.
DR AlphaFoldDB; I4N7X6; -.
DR STRING; 1179778.PMM47T1_07266; -.
DR PATRIC; fig|1179778.3.peg.1445; -.
DR eggNOG; COG0843; Bacteria.
DR OrthoDB; 9803294at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000004339; 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:UP000004339};
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..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 161..189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 201..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 320..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 353..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 390..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 426..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 467..490
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 26..530
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 530 AA; 58668 MW; 3D4676DBBC05F604 CRC64;
MSAVIDDHGH TGDDHAHGPA KGLMRWVLTT NHKDIGTLYL WFSFCMFLLG GSFAMVIRAE
LFQPGLQIVE PALFNQMTTM HGLVMVFGAV MPAFVGLANW MIPLMIGAPD MALPRMNNFS
FWLLPAAFLL LVSTLFSPGG GPNFGWTFYA PLSTTYAPAS VTFFIFAIHL MGISSIMGAI
NIIATILNLR APGMTLMKMP LFVWTWLITA FLLIAVMPVL AGCVTMMLMD IHFGTSFFSA
AGGGDPVLFQ HVFWFFGHPE VYIMILPAFG AISSIIPAFS RKPLFGYTSM VYATASIAFL
SFLVWAHHMF VVGIPLVGEL FFMYATMLIA VPTGVKVFNW ISTMWQGSLT FETPMLFAVA
FVILFTIGGF SGLMLAIAPA DFQYQDTYFV VAHFHYVLVP GAIFGIFASA YFWLPKWTGH
MYDETLGKLH FWLSFIGMNM AFFPMHFVGL AGMPRRVPDY NLQFANFNMV SSIGAFTFGA
TQIFFLFIVI KTIRGGPPAP AKPWDGAEGL EWTIPSPAPY HTFSTPPEVK
//
