ID H6MVJ6_GORPV Unreviewed; 579 AA.
AC H6MVJ6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:AFA74090.1};
GN OrderedLocusNames=GPOL_c30750 {ECO:0000313|EMBL:AFA74090.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74090.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA74090.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(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|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; CP003119; AFA74090.1; -; Genomic_DNA.
DR AlphaFoldDB; H6MVJ6; -.
DR STRING; 1112204.GPOL_c30750; -.
DR KEGG; gpo:GPOL_c30750; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_11; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000009154; 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 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 Oxidoreductase {ECO:0000313|EMBL:AFA74090.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154};
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 29..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 72..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 160..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 198..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 244..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 462..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 13..527
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT REGION 549..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64647 MW; 22FD43F1F29838F0 CRC64;
MAPVRPYPER HQPKGSFIYK LITTTDHKLI GMMYIVACFA FFLIGGLMAL LMRAELAHPG
MQFLSTEQFN QLFTMHGTVM LLMYATPIVI GFANFVLPLQ IGAPDVAFPR LNAFGFWLFV
FGSTIAIGGF ITPGGAADFG WTAYTPLTDA IHSPGVGADL WIMGLGVSGL GTILGGVNMV
TTVVCLRAPG MTMFRMPIFT WNILVTTILI LLIFPLLTAA LLGLEVDRQF GAHLYDPANG
GVILWQHLFW FFGHPEVYVI ALPFFGIVSE IFPVFSRKPL FGYSGLVYAT LAIAALSVAV
WAHHMYVTGA VLLPFFSFMT FLIAVPTGVK FFNWIGTMWK GHMTFETPML FSVGFIVTFL
FGGLTGVLLA SPPLDFHLSD SYFVVAHFHY VLFGTIVFAT YAGIYFWFPK MTGRMLDERL
GKWHFWLTFI GFHTTFLVQH WLGNEGMPRR YADYLPSDGF TTLNEVSTAG AFILGLSTLP
FLWNVFKSYR YGEVVTVDDP WGFGNSLEWA TSCPPPRHNF TELPRIRSER PAFELHYPHM
IDRMRAEAHV GPGHGHDSES AEHARRDPLT VGDHESSAD
//
