ID A0A2N1A1W0_9GAMM Unreviewed; 477 AA.
AC A0A2N1A1W0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN Name=ccoN {ECO:0000313|EMBL:PKG38720.1};
GN ORFNames=CXF74_12260 {ECO:0000313|EMBL:PKG38720.1};
OS Psychromonas sp. Urea-02u-13.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=2058326 {ECO:0000313|EMBL:PKG38720.1, ECO:0000313|Proteomes:UP000233836};
RN [1] {ECO:0000313|EMBL:PKG38720.1, ECO:0000313|Proteomes:UP000233836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Urea-02u-13 {ECO:0000313|EMBL:PKG38720.1,
RC ECO:0000313|Proteomes:UP000233836};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000256|PIRSR:PIRSR604677-50};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC Note=Binds 2 heme groups per subunit, denoted as high- and low-spin.
CC {ECO:0000256|PIRSR:PIRSR604677-50};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|ARBA:ARBA00009578, 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:PKG38720.1}.
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DR EMBL; PJBZ01000067; PKG38720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1A1W0; -.
DR OrthoDB; 9806838at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000233836; Unassembled WGS sequence.
DR GO; GO:0045278; C:plasma membrane 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01661; cbb3_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; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR NCBIfam; TIGR00780; ccoN; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422:SF29; CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID; 1.
DR Pfam; PF00115; COX1; 1.
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|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|PIRSR:PIRSR604677-50, ECO:0000256|RuleBase:RU000370};
KW Iron {ECO:0000256|PIRSR:PIRSR604677-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50};
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|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..477
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT BINDING 62
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 261
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 262
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 349
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2; high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 351
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
SQ SEQUENCE 477 AA; 53425 MW; 892049D26D45D05C CRC64;
MTTATTIQPD YNMKVVRQFT LTTILWGIIG MAVGVLIAAQ LVWPALNFDT PWLTYSRLRP
LHTNAVIFAF GTSALMATSF YVVQRTCQTR LFGGPLASIV FWGWQLVILS AVITLPLGYT
TSKEYAELEW PIDLLITAVW VVYAIVFFGT LTIRKTSHIY VANWFFGAFI LTVAVLHIVN
SMAIPVSLGS MKSYSIYAGA VDAMVQWWYG HNAVGFLLTA GFLGMMYYFV PKQANRPVYS
YRLSIIHFWA LIAVYIWAGP HHLHYTALPD WAQSLGMVMS LILFAPSWGG MINGIMTLSG
AWHKLRTDPI LRFLVVSLSF YGMSTFEGPM MAIKTVNALS HYTDWTVGHV HSGALGWVAM
VTIGAVYHLI PRLYGQKGMY SVALINLHFW MATIGTVLYI VAMWISGVMQ GLMWRAVNAD
GTLTYTFVES LEKSYPFYTI RFFGGLVFLS GMLIMAYNTY KTITAEKGSI QPQELGE
//
