ID D2ADX6_SHIF2 Unreviewed; 346 AA.
AC D2ADX6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Galactitol-1-phosphate dehydrogenase {ECO:0000313|EMBL:ADA74516.1};
GN Name=gatD {ECO:0000313|EMBL:ADA74516.1};
GN OrderedLocusNames=SFxv_2380 {ECO:0000313|EMBL:ADA74516.1};
OS Shigella flexneri serotype X (strain 2002017).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA74516.1, ECO:0000313|Proteomes:UP000001884};
RN [1] {ECO:0000313|EMBL:ADA74516.1, ECO:0000313|Proteomes:UP000001884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002017 {ECO:0000313|EMBL:ADA74516.1,
RC ECO:0000313|Proteomes:UP000001884};
RX PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT clone of Shigella flexneri.";
RL J. Clin. Microbiol. 48:419-426(2010).
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}.
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DR EMBL; CP001383; ADA74516.1; -; Genomic_DNA.
DR RefSeq; WP_000844251.1; NC_017328.1.
DR AlphaFoldDB; D2ADX6; -.
DR KEGG; sfe:SFxv_2380; -.
DR PATRIC; fig|591020.3.peg.2574; -.
DR HOGENOM; CLU_026673_11_0_6; -.
DR OMA; VYKIHNL; -.
DR Proteomes; UP000001884; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08236; sugar_DH; 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; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 6..344
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 37450 MW; D230CCE0B907123A CRC64;
MKSVVNDTDG IVRVAKSVIP EIKHQDEVRV KIASSGLCGS DLPRIFKNGA HYYPITLGHE
FSGYIDAVGS GVDDLHPGDA VACVPLLPCF TCPECLKGFY SQCAKYDFIG SRRDGGFAEY
IVVKRKNVFA LPTDMPIEDG AFIEPITVGL HAFHLAQGCE NKNVIIIGAG TIGLLAIQCA
VALGAKSVTA IDISSEKLAL AKSFGAMQTF NSSEMSAPQM QSVLRELRFN QLILETAGVP
QTVELAVEIA GPHAQLALVG TLHQDLHLTS ATFGKILRKE LTVIGSWMNY SSPWPGQEWE
TASRLLTERK LSLEPLIAHR GSFESFTQAV RDIARNAMQG KVLLIP
//