ID A0A1V9UBF3_9PSED Unreviewed; 544 AA.
AC A0A1V9UBF3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OQR27222.1};
GN ORFNames=BWR59_28725 {ECO:0000313|EMBL:OQR27222.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR27222.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR27222.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR27222.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
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:OQR27222.1}.
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DR EMBL; MUIN01000015; OQR27222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9UBF3; -.
DR STRING; 1943632.BWR59_28725; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000192462; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 255..269
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 544 AA; 59161 MW; 6AADDE76425C34FC CRC64;
MKTDFDYIIV GAGSSGCVLA NRLSADPAVS VCLIEAGSHD NNLRIQTPAG TITLYKSKKY
SWNFFSAPQK NLNGRSLHTP RGKALGGSSS MNSMIYIRGH ASDYDRWAEA GCPGWDWNSV
LPFFKKSENN RLGQDSRLHG FHGELNVEAA RDPNPVSQLF VKAAQKVGIR RNDDFNGEQL
EGCGIYNLTQ KDARRLSSYR AFVAPVLDRP NLTVITDCAV QSLILEQRVA KGVRVVSEGQ
QTRLTARREV ILSAGSLASP SLLLASGIGP AGELKNAGIK VEHDLPGVGR NLQDHLDGLI
TVRSKSPLTL GFSLGSLPSI LLSPLRYVLG KKGWLTTNYV EAGGFARTPL AEALPDVQFH
FVPGYRSHRG RLFEWGHGYA VHTCVLRPKS IGELRLDRSG KPVIDFNFLS DPEDAKVLIE
GLKLARKILA DQQFDGIRGI EMLPGKDVQT DEQLMTYVRE YAATVFHPVG TCKMGVDPMS
VVGPDLKVHG IEGLRVVDAS IMPTLISGNT NAPCIMIGEK AAEMILRGST QSAIKETTRS
AAIS
//
