ID A0A2M9R832_9FLAO Unreviewed; 727 AA.
AC A0A2M9R832;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cytochrome C oxidase Cbb3 {ECO:0000313|EMBL:PJR04893.1};
GN ORFNames=CDL10_10325 {ECO:0000313|EMBL:PJR04893.1};
OS Avrilella dinanensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Avrilella.
OX NCBI_TaxID=2008672 {ECO:0000313|EMBL:PJR04893.1, ECO:0000313|Proteomes:UP000231960};
RN [1] {ECO:0000313|EMBL:PJR04893.1, ECO:0000313|Proteomes:UP000231960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UR159 {ECO:0000313|EMBL:PJR04893.1,
RC ECO:0000313|Proteomes:UP000231960};
RA Leyer C., Sassi M., Minet J., Kayal S., Cattoir V.;
RT "Description of Avrilella dinanensis gen. nov. sp. nov.";
RL Submitted (JUN-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 -!- 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:PJR04893.1}.
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DR EMBL; NIPO01000001; PJR04893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9R832; -.
DR OrthoDB; 9806838at2; -.
DR Proteomes; UP000231960; 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:0009060; P:aerobic respiration; IEA:InterPro.
DR CDD; cd01661; cbb3_Oxidase_I; 1.
DR Gene3D; 6.10.250.2250; -; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
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 InterPro; IPR003468; Cyt_c_oxidase_monohaem-su/FixO.
DR NCBIfam; TIGR00780; ccoN; 1.
DR NCBIfam; TIGR00781; ccoO; 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 Pfam; PF02433; FixO; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR604677-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604677-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604677-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000231960};
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 16..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..465
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT DOMAIN 535..718
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 59
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 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 256
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 344
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 346
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 727 AA; 82800 MW; 3AA5996CE566F83C CRC64;
MEVQQFYYDN KIVKKFLYAT IAYGVIGMAV GLLLALLFIF PNLTEGISWL SFGRLRPLHT
NAVIFAFVGN AIFAGVYYSL QRLLKARMYS DFLSNLNFWG WQLVIISAVI TLPLGYSSSK
EYAELEWPID IAIAIVWVAF GLNMIMTILR RRERHLYVAI WFYLGTFVTV AVLHIFNSLA
LPVSGLKSYS VYAGVQDALV QWWYGHNAVA FFLTTPFLGL MYYYLPKAAN RPIYSYRLSI
IHFWSLIFLY IWAGPHHLLY TALPEWAQNL GVVFSVMLLA PSWGGMINGL LTLRGAWDKV
RTDPILKFFV VAITGYGMAT FEGPMLSLKN VNAIAHYTDW IIAHVHVGAL AWNGFMTFGI
IYWLIPRMVK TKLYSQALAN FHFWIGTLGI VLYCIPLYVA GFQQHLMWKE FTPDGMLKYG
NFMDTVTAIM PMYAMRAAGG SLYLVGMIIL VYNIYKTIRA GQKVEDEMAE APALAVISKN
RVKGEGWHSW LERKPIQLTV LATITILIGG IVQIVPTLVV ESNIPTIESV KPYTPLELVG
RDLYIREGCV GCHSQMIRPF RSEVERYGEY SKSGEYVYDH PFLWGSKRTG PDLHRVGGKY
SDNWHFNHMY DPQSTSTGSI MPSYKWLFAN KSMYYDDIEK KMEVLATLGA PYTEEDIAQA
RENIKIQGEQ IAKNLETDPD YVKSYEESKK TAQARGEEFV PMSQREITAL IAYLQRLGTD
IKVKDAN
//
