GDH_RHIL3
ID GDH_RHIL3 Reviewed; 257 AA.
AC Q1MLL4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Galactitol 2-dehydrogenase {ECO:0000303|PubMed:24731824};
DE Short=GDH {ECO:0000303|PubMed:24731824};
DE EC=1.1.1.16 {ECO:0000269|PubMed:24731824};
DE AltName: Full=RlGDH {ECO:0000303|PubMed:24731824};
GN Name=gdh {ECO:0000303|PubMed:24731824};
GN OrderedLocusNames=RL0645 {ECO:0000312|EMBL:CAK06139.1};
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=3841;
RX PubMed=24731824; DOI=10.1016/j.enzmictec.2014.02.012;
RA Jagtap S.S., Singh R., Kang Y.C., Zhao H., Lee J.K.;
RT "Cloning and characterization of a galactitol 2-dehydrogenase from
RT Rhizobium legumenosarum and its application in D-tagatose production.";
RL Enzyme Microb. Technol. 58:44-51(2014).
CC -!- FUNCTION: Catalyzes the oxidation of galactitol to D-tagatose. Also
CC catalyzes the oxidation of a wide range of substrates, including
CC polyvalent aliphatic alcohols and polyols, to the corresponding ketones
CC and ketoses. Galactitol is the preferred substrate.
CC {ECO:0000269|PubMed:24731824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactitol + NAD(+) = H(+) + keto-D-tagatose + NADH;
CC Xref=Rhea:RHEA:20685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16813,
CC ChEBI:CHEBI:47693, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.16;
CC Evidence={ECO:0000269|PubMed:24731824};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24731824};
CC Note=Binds one Mg(2+) per dimer. Can also use other divalent cations.
CC {ECO:0000269|PubMed:24731824};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.8 mM for galactitol {ECO:0000269|PubMed:24731824};
CC KM=1 mM for NAD(+) {ECO:0000269|PubMed:24731824};
CC Note=kcat is 835 min(-1). {ECO:0000269|PubMed:24731824};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:24731824};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:24731824};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:24731824}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AM236080; CAK06139.1; -; Genomic_DNA.
DR RefSeq; WP_011650422.1; NC_008380.1.
DR AlphaFoldDB; Q1MLL4; -.
DR SMR; Q1MLL4; -.
DR STRING; 216596.RL0645; -.
DR EnsemblBacteria; CAK06139; CAK06139; RL0645.
DR KEGG; rle:RL0645; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_1_5; -.
DR OMA; QFSMKGK; -.
DR OrthoDB; 1294334at2; -.
DR BRENDA; 1.1.1.16; 5343.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0047713; F:galactitol 2-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019402; P:galactitol metabolic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; Oxidoreductase.
FT CHAIN 1..257
FT /note="Galactitol 2-dehydrogenase"
FT /id="PRO_0000446638"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 21..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 67..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
SQ SEQUENCE 257 AA; 27289 MW; AD772AC7C97D8A29 CRC64;
MSYQQKFRLD GERAVVTGGG RAIGLCCTEA LAEAGAAVVV IERSEADAEQ ALALRNRGYD
VEVRVGDVTD AARMDAIATE LADGGRPATI LVNNAGIGQS GIPAQDLTDA DWLRMMDVNL
NGVFWCSRAF GRSMISMKRG AIVNLGSMSG TICNRPQPQT AYNVSKAAVH HLTRSLAAEW
AHHGIRVNAV APTYIETPMV VAVEANRERI PLWLADTPMA RMGTPEEVAS AVLFLASGAA
SLMTGAIVNV DAGFTCW
