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Database: UniProt
Entry: A0A1I6ELW9_9RHOB
LinkDB: A0A1I6ELW9_9RHOB
Original site: A0A1I6ELW9_9RHOB 
ID   A0A1I6ELW9_9RHOB        Unreviewed;       554 AA.
AC   A0A1I6ELW9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SFR18637.1};
GN   ORFNames=SAMN04515673_11450 {ECO:0000313|EMBL:SFR18637.1};
OS   Poseidonocella sedimentorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Poseidonocella.
OX   NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR18637.1, ECO:0000313|Proteomes:UP000199302};
RN   [1] {ECO:0000313|EMBL:SFR18637.1, ECO:0000313|Proteomes:UP000199302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC   {ECO:0000313|Proteomes:UP000199302};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FOYI01000014; SFR18637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6ELW9; -.
DR   STRING; 871652.SAMN04515673_11450; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000199302; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199302}.
FT   DOMAIN          276..290
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          138..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         236
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   554 AA;  60481 MW;  6CF1E4D8956A68AE CRC64;
     MADAATEVDF IVIGGGSAGC LLANRLSADA ANRVLLLEAG KADSYPWIHV PVGYLYCIGN
     PRTDWMYTTE ADAGLNGRTL RYPRGKTLGG CSSINGMIYM RGQARDYDNW AALTGEEDWS
     WENALQDFKA HENHYKLDGG ADPRTGDNER FSDTHGHGGE WRVEKQRLRW DVLDSFADAA
     VEAGIEKTDD FNSGDNAGVG YFDVNQRSGW RWNTSKAFLK PAKTRRNLTI WTESQVEKLT
     FERDADGKLR CSGATVNRKG KTLTVTARRE TVLSAGAINS PQILQLSGIG PADLLRAHGI
     EVLRDAPVGE NLQDHLQIRA VYKVNGTSTL NALASTLFGK AKIGAEYALK RSGPMSMAPS
     QLGAFTRSDP NRSHANLEYH VQPLSLDAFG EPLHAFPAMT VSVCNLNPTS RGNVRIRSAN
     FRDAPMISPN YLATEDDRKV AADSLRQVRE IMAQPAMASY RPEEYKPGVQ YQSDEDLAKL
     AGDIANTIFH PVGTVKMGGS EDDSAVLDPH LRLKGVAGLR VVDASIMPEI TSGNTNSPTL
     MIAEKAARWI LAGH
//
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