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Database: UniProt
Entry: I3CM64_9BURK
LinkDB: I3CM64_9BURK
Original site: I3CM64_9BURK 
ID   I3CM64_9BURK            Unreviewed;       543 AA.
AC   I3CM64;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EIJ44707.1};
GN   ORFNames=GWL_41460 {ECO:0000313|EMBL:EIJ44707.1};
OS   Herbaspirillum sp. GW103.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1175306 {ECO:0000313|EMBL:EIJ44707.1, ECO:0000313|Proteomes:UP000004194};
RN   [1] {ECO:0000313|EMBL:EIJ44707.1, ECO:0000313|Proteomes:UP000004194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW103 {ECO:0000313|EMBL:EIJ44707.1,
RC   ECO:0000313|Proteomes:UP000004194};
RX   PubMed=22815460; DOI=10.1128/JB.00806-12;
RA   Lee G.W., Lee K.J., Chae J.C.;
RT   "Genome sequence of Herbaspirillum sp. strain GW103, a plant growth-
RT   promoting bacterium.";
RL   J. Bacteriol. 194:4150-4150(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:EIJ44707.1}.
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DR   EMBL; AJVC01000006; EIJ44707.1; -; Genomic_DNA.
DR   RefSeq; WP_008333842.1; NZ_AJVC01000006.1.
DR   AlphaFoldDB; I3CM64; -.
DR   STRING; 1175306.GWL_41460; -.
DR   PATRIC; fig|1175306.3.peg.4032; -.
DR   eggNOG; COG2303; Bacteria.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000004194; 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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968}.
FT   DOMAIN          82..105
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          260..274
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   543 AA;  58908 MW;  E3788A620A609991 CRC64;
     MLFDYVIVGG GSAGATLAAR LSEDPGVTVC LLEAGGQGDS LLVRTPAAVV AMLPGYGKLN
     NWALQTTPQP GLNGRRGYQP RGRALGGSSA INAMLYIRGQ RQDYDGWAQA GCPGWDWESV
     LPYFKRSENN IRGADAWHGD SGPLQVSEQN RPRPITRAFI EAAQARGYPL CTDFNTGDNE
     GVGLYQVTQF HTPAHRGERC SAAAAYLHPV MGQRPNLSVL RQVRAQRVLF EGKRAVGVAY
     RQQQQDAQVR ATREVILAAG AFGSPQLLQL SGVGRPEDIL PHGIALHHAL PGVGQNLQDH
     LDFTQGWTTR DTDNFGLGVV GGLRLLGQLL PWKRHGEGLI ATPFAEGAAF LKTRTGLDRP
     DIQLHFCIAI VDDHARKLHA GYGFSLHMCL LRPHSRGRVG LQSADAMADP LIDAGYLSDP
     RDLPTMIEGA RIARDIVMTE PLRRYCRREL FGGREGMDEA AWEAMIRRRA DTIYHPVGTC
     RMGADPMAVV DAQLRVHGLH GLRVVDASVM PTLVSGNTNA PTIMIAEKAA DMIRASQAHA
     EAA
//
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