ID A0A0S8AYC0_9PROT Unreviewed; 540 AA.
AC A0A0S8AYC0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KPK04311.1};
GN ORFNames=AMJ64_13970 {ECO:0000313|EMBL:KPK04311.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK04311.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK04311.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK04311.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK04311.1}.
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DR EMBL; LJTQ01000175; KPK04311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AYC0; -.
DR STRING; 1703390.AMJ64_13970; -.
DR PATRIC; fig|1703390.3.peg.1009; -.
DR Proteomes; UP000051483; 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}.
FT DOMAIN 263..277
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 540 AA; 59114 MW; 667CDFAFD193A1BC CRC64;
MSDTPFGTFD YIVIGAGSAG CLLANRLSAD PQRSVLLLEA GGDDDWVWIR IPIGYLYTIG
NPRTDWCYQT APDEHLAGRS LLYARGRVLG GCSSINAMIY MRGQKDDWDH WSALGNRGWS
WDEVLPVFQR LEDYQYGNAD AYGTGGELRV EDPRVAWEIL DAWRAAAAEC GIPAVKAFNG
GDNFGCAYFQ MNQRVGRRWS ATDAFLKPVR QRGNLTVLPN ALVRRLRIEV QDGVRRCTGV
EFAHPEHGTR VAAARRETLL AAGAIGSPQL LQLSGVGPAA LLGAHGIPLA HDLPGVGENL
HDHLQIRMQY KVSNVRTMNA LANSALSRMM MGAQYFLFRS GPLTMPPSQL GAFARSDASQ
PTPNIEWHVQ PLSLDKFGDP LHPFPAITPS VCNLRPTSRG WVRITSPDPE TYPEIKLNYL
STEEDRRIAA DAMRFTRRIM AAKALSRYNP VEFRPGGAAR SGEALARAAG ELGTTIFHPV
GTCRMGHDPL AVVDDRLRVH GVEALRVIDA SVMPRITSGN TNAPTYVIAE KGAAFVLEAG
//
