ID A0A1T0CTK1_9GAMM Unreviewed; 489 AA.
AC A0A1T0CTK1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN ORFNames=B0680_02305 {ECO:0000313|EMBL:OOS25676.1};
OS Moraxella pluranimalium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=470453 {ECO:0000313|EMBL:OOS25676.1, ECO:0000313|Proteomes:UP000189800};
RN [1] {ECO:0000313|EMBL:OOS25676.1, ECO:0000313|Proteomes:UP000189800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 54913 {ECO:0000313|EMBL:OOS25676.1,
RC ECO:0000313|Proteomes:UP000189800};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella pluranimalium CCUG 54913T type
RT strain.";
RL Submitted (FEB-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:OOS25676.1}.
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DR EMBL; MUYU01000006; OOS25676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CTK1; -.
DR STRING; 470453.B0680_02305; -.
DR OrthoDB; 9806838at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000189800; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000189800};
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..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..489
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT BINDING 68
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 215
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 265
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 266
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 353
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 355
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 489 AA; 54503 MW; A3E3C0B54F06B6FC CRC64;
MSLYKSAVAP LSVDHEYEIT IVRLFTIMAV VWGIVGMTVG VFIASQLAWP VLNFDTSWLS
FGRLRPLHTN AVIFAFGGSA LFATSYYIVQ RTCKTRLFAP YLAWFTFWGW QAIIIAAVIT
LPLGITSAKE YAELEWPIDI AIALVWVAYA IVFFGTIIKR QTSHIYVANW FFAAFIITIA
LLHIVNSFAV PVGLWKSYSL FGGATDAMVQ WWYGHNAVGF YLTAAFLGMM YYFIPVQVGR
PVYSYRLSIV HFWALIASYM WAGGHHLHYS ALPDWTQSLG MVFSLILFAP SWGGMINGVL
TLSGSWDKLR TDPIIRFLIV ALSFYAMSTF EGPMLSIKAV NAISHNTDWT VGHVHSGALG
WVGMVTIGSI YVLLPRIYNK AKMYSTSLIM LHFWLATTGT VLYIVALWIS GITQGMMWRA
TNPDGTLAYD FIQTVVVSHW PFVVRALGGA LYVAGMVVMA YNCYRTIKMP SVVEPAAEKQ
ADDAATAQA
//
