ID A0A1X6ZB67_9RHOB Unreviewed; 539 AA.
AC A0A1X6ZB67;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Alcohol dehydrogenase [acceptor] {ECO:0000313|EMBL:SLN45899.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:SLN45899.1};
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:PSK86439.1};
GN Name=alkJ {ECO:0000313|EMBL:SLN45899.1};
GN ORFNames=CLV79_105146 {ECO:0000313|EMBL:PSK86439.1}, LOS8367_02026
GN {ECO:0000313|EMBL:SLN45899.1};
OS Limimaricola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN45899.1, ECO:0000313|Proteomes:UP000193495};
RN [1] {ECO:0000313|EMBL:SLN45899.1, ECO:0000313|Proteomes:UP000193495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN45899.1,
RC ECO:0000313|Proteomes:UP000193495};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSK86439.1, ECO:0000313|Proteomes:UP000240624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK86439.1,
RC ECO:0000313|Proteomes:UP000240624};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; PYGB01000005; PSK86439.1; -; Genomic_DNA.
DR EMBL; FWFY01000005; SLN45899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ZB67; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000193495; Unassembled WGS sequence.
DR Proteomes; UP000240624; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000313|EMBL:SLN45899.1}.
FT DOMAIN 81..104
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 253..267
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 539 AA; 58578 MW; 89145FE40E8036DC CRC64;
MAVSDYIIIG AGSAGCVLAE RLSASGRYSV LVLEAGPRDR SPWVRLPLGY GKTFFHPRLN
WRYRSAPDPG LNGRSDYWPR GRVVGGSSSI NALIWARGLP HDFDDWAADG AEGWDWDAAR
RAFEAMETRV AADGSRDGSG PLHVQDVSDQ IHPVTRHFFD GMAQAGLPAC PDCNGARFEG
ATTYRITTRS GLRHSAARAY LAPALRRSNV TLRTGVTVTR IGFEGRRAAT VELRIGDRIE
TLRAGREILL CAGAVTSPRL LQLSGIGPAE LLRAHGIEVL ADAPHVGGQL QDHLAVNYYF
KANEPTLNDQ LRPFWGKARA AIRYALSRRG PLALSVNQCG GFFRGTAESP QPDQQIYFNP
VSYSTTPTGR RDLVRPDPFP GFIISFQPAR PTSRGRIDIS SADPLAPPDI RPNSLATEAD
RETVIAGGQL CRRIMRSPAL TALVESAVDP DLRALDGAAI LDDFRDRCGT VFHPVGTCRM
GADPRRSVVD PRLRLHGFDG LRVVDASVFP SITSGNTNAP TMMVAHRAAE MVLDDARTT
//
