ID A0A0D6T2T7_9PSED Unreviewed; 361 AA.
AC A0A0D6T2T7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2,3-butanediol dehydrogenase, R-alcohol forming, (R)-and (S)-acetoin-specific {ECO:0000313|EMBL:KIV74848.1};
DE EC=1.1.1.4 {ECO:0000313|EMBL:KIV74848.1};
GN ORFNames=SZ55_0417 {ECO:0000313|EMBL:KIV74848.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV74848.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV74848.1, ECO:0000313|Proteomes:UP000032531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV74848.1,
RC ECO:0000313|Proteomes:UP000032531};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:KIV74848.1}.
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DR EMBL; JYFT01000005; KIV74848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6T2T7; -.
DR PATRIC; fig|1604022.3.peg.433; -.
DR Proteomes; UP000032531; Unassembled WGS sequence.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08233; butanediol_DH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KIV74848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032531};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 15..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 38372 MW; 363CAD968D34C99C CRC64;
MSILPNSMRA AVWHGRNDIR VEDVPLPGDP APGWVQIRVH WCGICGSDLH EYVAGPVFIP
VEAPHPLTGI KGQCILGHEF CGEIVKLGDG VQGFTPGEVV AADACQHCGT CYYCRHGLYN
ICENLAFTGL MNNGAFAEWV NVPANLLYKL PAGFPAEAGA LIEPLAVGMH AVKKAGSLLG
RNVVVVGAGT IGLCTIMCAR AAGAAQVIAL EMSSARKAKA REVGASHVLD PNECDVLAEI
RTLTQGLGAD VSFECIGNKH TAKLAIDAIR KAGTCVLVGI FEEPSSFNFF ELVATEKQVL
GALAYNGEFA DVIAFIADGR LDITPLVTGR IELEQIVEKG FEELVHNKEH NVKIIVSPRA
A
//
