GATD_ECOLI
ID GATD_ECOLI Reviewed; 346 AA.
AC P0A9S3; P37190; P76410;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Galactitol 1-phosphate 5-dehydrogenase;
DE EC=1.1.1.251 {ECO:0000269|PubMed:13331868};
GN Name=gatD; OrderedLocusNames=b2091, JW2075;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC3132;
RX PubMed=7772602; DOI=10.1016/0167-4781(95)00053-j;
RA Nobelmann B., Lengeler J.W.;
RT "Sequence of the gat operon for galactitol utilization from a wild-type
RT strain EC3132 of Escherichia coli.";
RL Biochim. Biophys. Acta 1262:69-72(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=13331868; DOI=10.1128/jb.71.5.557-564.1956;
RA Wolff J.B., Kaplan N.O.;
RT "Hexitol metabolism in Escherichia coli.";
RL J. Bacteriol. 71:557-564(1956).
CC -!- FUNCTION: Converts galactitol 1-phosphate to D-tagatose 6-phosphate.
CC {ECO:0000269|PubMed:13331868}.
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:0000269|PubMed:13331868};
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 -!- INTERACTION:
CC P0A9S3; P0A9S3: gatD; NbExp=3; IntAct=EBI-1127517, EBI-1127517;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X79837; CAA56231.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75152.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15954.1; -; Genomic_DNA.
DR PIR; B64976; B64976.
DR RefSeq; NP_416594.1; NC_000913.3.
DR RefSeq; WP_000844219.1; NZ_SSZK01000011.1.
DR PDB; 4A2C; X-ray; 1.87 A; A/B=1-346.
DR PDB; 4UEJ; X-ray; 1.74 A; A/B=1-346.
DR PDB; 4UEK; X-ray; 1.90 A; A/B=1-346.
DR PDB; 4UEO; X-ray; 2.00 A; A/B=1-346.
DR PDBsum; 4A2C; -.
DR PDBsum; 4UEJ; -.
DR PDBsum; 4UEK; -.
DR PDBsum; 4UEO; -.
DR AlphaFoldDB; P0A9S3; -.
DR SMR; P0A9S3; -.
DR BioGRID; 4260429; 17.
DR DIP; DIP-47890N; -.
DR IntAct; P0A9S3; 17.
DR MINT; P0A9S3; -.
DR STRING; 511145.b2091; -.
DR jPOST; P0A9S3; -.
DR PaxDb; P0A9S3; -.
DR PRIDE; P0A9S3; -.
DR EnsemblBacteria; AAC75152; AAC75152; b2091.
DR EnsemblBacteria; BAA15954; BAA15954; BAA15954.
DR GeneID; 66674013; -.
DR GeneID; 946598; -.
DR KEGG; ecj:JW2075; -.
DR KEGG; eco:b2091; -.
DR PATRIC; fig|1411691.4.peg.159; -.
DR EchoBASE; EB2316; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR InParanoid; P0A9S3; -.
DR OMA; AYCYSTE; -.
DR PhylomeDB; P0A9S3; -.
DR BioCyc; EcoCyc:GALACTITOLPDEHYD-MON; -.
DR BioCyc; MetaCyc:GALACTITOLPDEHYD-MON; -.
DR BRENDA; 1.1.1.251; 2026.
DR PRO; PR:P0A9S3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008868; F:galactitol-1-phosphate 5-dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0019404; P:galactitol catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Galactitol metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..346
FT /note="Galactitol 1-phosphate 5-dehydrogenase"
FT /id="PRO_0000160879"
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"
FT CONFLICT 213
FT /note="S -> L (in Ref. 1; CAA56231)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> G (in Ref. 1; CAA56231)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..227
FT /note="EL -> DV (in Ref. 1; CAA56231)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="A -> T (in Ref. 1; CAA56231)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..329
FT /note="AQA -> TQV (in Ref. 1; CAA56231)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4UEJ"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4UEJ"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4UEJ"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:4UEJ"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:4UEJ"
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
