ID A0A0U2YXF5_9MICC Unreviewed; 570 AA.
AC A0A0U2YXF5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN Name=ctaD1 {ECO:0000313|EMBL:GEO93248.1};
GN ORFNames=AS188_10930 {ECO:0000313|EMBL:ALU40177.1}, KFL01_25540
GN {ECO:0000313|EMBL:GEO93248.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU40177.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU40177.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU40177.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO93248.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO93248.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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; CP013254; ALU40177.1; -; Genomic_DNA.
DR EMBL; BJZR01000097; GEO93248.1; -; Genomic_DNA.
DR RefSeq; WP_058858878.1; NZ_JALJPS010000001.1.
DR AlphaFoldDB; A0A0U2YXF5; -.
DR STRING; 446860.AS188_10930; -.
DR KEGG; kfv:AS188_10930; -.
DR OrthoDB; 9803294at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000057181};
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 83..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 170..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 208..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 254..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 290..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 392..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 472..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 30..537
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63639 MW; 14A212E16DE792C8 CRC64;
MSTLEYSRDE AAAVAPRVVP RSKGRLIVNW ITSTDHKTIG YMYLISSFTF FCIAGVMALL
IRAELFEPGM QVLETKEQYN QLFTMHGTLM LLMFGTPLFA GFANVIVPLQ IGAPDVAFPR
LNALAFWFFL FGSLVALAGF ITPQGAASFG WFAYTPLSNS SFSPGAGGNL WVFGLALQGF
GTIMGAVNFI TTIIAMRAPG MTVWRMGLFT WNALITSLLI VMVFPPLAAA LFALGMDRTL
GGHIFDPANG GAVLWQHLFW FFGHPEVYVL ALPFFGIVSE IIPVFSRKPL FGYKGLVFAT
IAIAALSVTV WAHHMYVTGA VMLSFFAFMT MMIAVPTGVK FFNWIGTMWQ GSITFETPML
WVLGFLFTFL FGGLTGVILA TPPLDFHVSD SYFVVAHFHY VVFGTVVFGM FAGFYFWWPK
WTGYMLNERI GKIHFWLLFL GFHMTFLIQH WLGVDGMPRR YADYLPEDGF TWMNQISTVG
SMLLGVSMIP FFYNVWTTHR NGKKVEVDDP WGFGGSLEWA TSCPPPRHNF TSLPRIRSER
PALDLHHPEL AAESPQQSPV DDAAMATRKG
//
