ID A0A1H8C7I3_9SPHN Unreviewed; 553 AA.
AC A0A1H8C7I3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN ORFNames=SAMN05192583_1471 {ECO:0000313|EMBL:SEM90404.1};
OS Sphingomonas gellani.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEM90404.1, ECO:0000313|Proteomes:UP000199206};
RN [1] {ECO:0000313|Proteomes:UP000199206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA Varghese N., Submissions S.;
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|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; FOCF01000003; SEM90404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8C7I3; -.
DR STRING; 1166340.SAMN05192583_1471; -.
DR OrthoDB; 9803294at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000199206; 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:UP000199206};
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 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 98..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 144..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 223..250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 270..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 306..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 342..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 499..516
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 553 AA; 61092 MW; 96096A2961D304E8 CRC64;
MTDTALHPSA FQAHDHGHHD HAEHKPAFFA RWFMSTNHKD IGTLYLIFAI VAGIIGGAIS
GLMRAELAHP GIQYLGTWAR LLHGGEQSLD QSLHLWNVLI TAHGLIMVFF MVMPAMIGGF
GNWFVPIMIG APDMAFPRMN NISFWLLIPA FTLLLASPFL GGAGVGWTAY APLSTYGEPG
PSVDMAILSL HLAGASSIMG AINFITTIFN MRAPGMTLHK MPLFVWSVLV TAFLLLLSLP
VLAAAITMLL TDRNFGTTFF DPAGGGDPVL YQHLFWFFGH PEVYIMILPG FGIISQIIAT
FSRKPVFGYL GMAYAMVAIG VVGFVVWAHH MFATGLSVNT KMYFTAATMV IAVPTGIKIF
SWIATMWGGS ISFKTPMVWA IGFIFMFTVG GVTGVVLANG GVDDYMQDTY YVVAHFHYVL
SLGAVFALFA GFYYWFPKMS GKMYSEFLGQ LHFWVFFVGV NVLFFPMHFL GLQGMPRRYP
DYPDAYATWN AMASHGYEIM TVGMVIFFVN VIWSLIAGKK ADDNPWGEGA TTLEWTLSSP
PPYHQFETLP RID
//
