GATD_ECO57
ID GATD_ECO57 Reviewed; 346 AA.
AC P0A9S4; P37190; P76410;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Galactitol 1-phosphate 5-dehydrogenase;
DE EC=1.1.1.251 {ECO:0000250|UniProtKB:P0A9S3};
GN Name=gatD; OrderedLocusNames=Z3254, ECs2894;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Converts galactitol 1-phosphate to tagatose 6-phosphate.
CC {ECO:0000250|UniProtKB:P0A9S3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactitol 1-phosphate + NAD(+) = H(+) + keto-D-tagatose 6-
CC phosphate + NADH; Xref=Rhea:RHEA:28106, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60083,
CC ChEBI:CHEBI:134283; EC=1.1.1.251;
CC Evidence={ECO:0000250|UniProtKB:P0A9S3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57148.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36317.1; -; Genomic_DNA.
DR PIR; F90990; F90990.
DR PIR; H85835; H85835.
DR RefSeq; NP_310921.1; NC_002695.1.
DR RefSeq; WP_000844219.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9S4; -.
DR SMR; P0A9S4; -.
DR STRING; 155864.EDL933_3160; -.
DR EnsemblBacteria; AAG57148; AAG57148; Z3254.
DR EnsemblBacteria; BAB36317; BAB36317; ECs_2894.
DR GeneID; 66674013; -.
DR GeneID; 916596; -.
DR KEGG; ece:Z3254; -.
DR KEGG; ecs:ECs_2894; -.
DR PATRIC; fig|386585.9.peg.3026; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR OMA; AYCYSTE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008868; F:galactitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019402; P:galactitol metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Galactitol metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..346
FT /note="Galactitol 1-phosphate 5-dehydrogenase"
FT /id="PRO_0000160880"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37390 MW; B35A2B004E5A4032 CRC64;
MKSVVNDTDG IVRVAESVIP 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 GSFESFAQAV RDIARNAMPG KVLLIP
