ID I4N3Z3_9PSED Unreviewed; 538 AA.
AC I4N3Z3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Alcohol dehydrogenase (Acceptor) {ECO:0000313|EMBL:EIK96183.1};
GN ORFNames=PMM47T1_12863 {ECO:0000313|EMBL:EIK96183.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK96183.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK96183.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK96183.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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:EIK96183.1}.
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DR EMBL; AJWX01000010; EIK96183.1; -; Genomic_DNA.
DR RefSeq; WP_008369339.1; NZ_AJWX01000010.1.
DR AlphaFoldDB; I4N3Z3; -.
DR STRING; 1179778.PMM47T1_12863; -.
DR PATRIC; fig|1179778.3.peg.2582; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000004339; 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 Reference proteome {ECO:0000313|Proteomes:UP000004339}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 252..266
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 538 AA; 57961 MW; 80C764B48D0CBB19 CRC64;
MNTDFDYIIV GAGSSGCVLA NRLSADPQVK VCLIEAGGND NSPRIQTPAG TITLYKSKKY
SWNFFSAPQK NLGNRSLHTP RGKALGGSSS MNSMIYIRGH ASDYDRWAQP GWDWASVLPY
FKQSENNRLG QDPALHGTGG ELNVEAARDP NPVSGMFVKA AEKIGIRRND DFNGPRLEGC
GIYNLTQKTA RRLSSYRAFV APVLDRTNLT VVTDCTVKSV VVEQKIAKGV VVDSNGVQTF
LKARREVILS AGAIGSPQLL LASGIGPAAE LTEAGIPVRH DLPGVGKNLQ DHLDGLVTVR
SKSPLTLGFS LGSLAAILAS PLRYLVSKMG WLTTNYVEAG GFARTPLAEA LPDVQFHFVP
GYRSHRGRLF EWGHGYAVHT CVLRPKSIGE LRLGRDGTLV IDFNFLSNPD DAKVLVEGLK
LARRILADTQ FDAIRGKEML PGAQVQTDQQ LLDYVRDYAA TVFHPVGTCK MGSDPMAVVD
PQLRVHGIRG LRVVDASIMP TLISGNTNAP CIMIGEKAAA MILEPANATA NAAKMAAI
//
