GATDH_CERSP
ID GATDH_CERSP Reviewed; 254 AA.
AC C0KTJ6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Galactitol 2-dehydrogenase (L-tagatose-forming) {ECO:0000305};
DE EC=1.1.1.406 {ECO:0000269|PubMed:7551050};
DE AltName: Full=Galactitol dehydrogenase {ECO:0000303|PubMed:7551050};
DE Short=GDH {ECO:0000303|PubMed:7551050};
DE Short=GatDH {ECO:0000303|PubMed:19778027};
DE AltName: Full=Galactitol:NAD(+) 5-oxidoreductase {ECO:0000303|PubMed:19778027};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 8371 / Si4, and DSM 8371 / Si4 / D;
RA Kohring G.W., Kornberger P., Zimmer C.L., Giffhorn F.;
RT "Investigations on modified regulation of the galactitol-dehydrogenase gene
RT from Rhodobacter sphaeroides strain D compared to strains Si4 and 2.4.1 and
RT electroenzymatic application potential of the GatDH enzyme.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=DSM 8371 / Si4 / D;
RX PubMed=7551050; DOI=10.1099/13500872-141-8-1865;
RA Schneider K.H., Jakel G., Hoffmann R., Giffhorn F.;
RT "Enzyme evolution in Rhodobacter sphaeroides: selection of a mutant
RT expressing a new galactitol dehydrogenase and biochemical characterization
RT of the enzyme.";
RL Microbiology 141:1865-1873(1995).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=DSM 8371 / Si4 / D;
RX PubMed=15296184;
RA Kohring G.W., Wiehr P., Jeworski M., Giffhorn F.;
RT "Stereoselective oxidation of aliphatic diols and reduction of hydroxy-
RT ketones with galactitol dehydrogenase from Rhodobacter sphaeroides D.";
RL Commun. Agric. Appl. Biol. Sci. 68:309-312(2003).
RN [4]
RP BIOTECHNOLOGY.
RC STRAIN=DSM 8371 / Si4 / D;
RX PubMed=19778027; DOI=10.1021/la9010168;
RA Kornberger P., Gajdzik J., Natter H., Wenz G., Giffhorn F., Kohring G.W.,
RA Hempelmann R.;
RT "Modification of galactitol dehydrogenase from Rhodobacter sphaeroides D
RT for immobilization on polycrystalline gold surfaces.";
RL Langmuir 25:12380-12386(2009).
RN [5] {ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB, ECO:0007744|PDB:3LQF}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEXES WITH NAD; MAGNESIUM AND
RP SUBSTRATES, SUBUNIT, AND ACTIVE SITE.
RC STRAIN=DSM 8371 / Si4 / D;
RX PubMed=20410293; DOI=10.1074/jbc.m110.113738;
RA Carius Y., Christian H., Faust A., Zander U., Klink B.U., Kornberger P.,
RA Kohring G.W., Giffhorn F., Scheidig A.J.;
RT "Structural insight into substrate differentiation of the sugar-
RT metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides
RT D.";
RL J. Biol. Chem. 285:20006-20014(2010).
CC -!- FUNCTION: Catalyzes the interconversion of galactitol to the rare sugar
CC L-tagatose (PubMed:7551050). Shows activity with a wide range of
CC substrates, and catalyzes the oxidation of a variety of polyvalent
CC aliphatic alcohols and polyols to the corresponding ketones and
CC ketoses, respectively, and in the reverse reaction, it reduces ketones
CC with high stereoselectivity yielding the corresponding S-configurated
CC alcohols (PubMed:7551050, PubMed:15296184). Shows high activity with D-
CC threitol, xylitol, 1,2-hexanediol, 1,2-pentanediol, 2-hexanol, L-
CC erythrulose, D-ribulose and acetoin (PubMed:7551050). Specific for
CC NAD(+) (PubMed:7551050). {ECO:0000269|PubMed:15296184,
CC ECO:0000269|PubMed:7551050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactitol + NAD(+) = H(+) + keto-L-tagatose + NADH;
CC Xref=Rhea:RHEA:51688, ChEBI:CHEBI:15378, ChEBI:CHEBI:16813,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:134275;
CC EC=1.1.1.406; Evidence={ECO:0000269|PubMed:7551050};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:7551050};
CC Note=Can use Mg(2+), Mn(2+), Ni(2+) or Co(2+).
CC {ECO:0000269|PubMed:7551050};
CC -!- ACTIVITY REGULATION: Inhibited by the chelating agents EDTA and
CC alpha,alpha'-dipyridyl (PubMed:7551050). Inhibited by Zn(2+) and Fe(2+)
CC (PubMed:7551050). {ECO:0000269|PubMed:7551050}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=240 mM for galactitol {ECO:0000269|PubMed:7551050};
CC KM=85 mM for D-threitol {ECO:0000269|PubMed:7551050};
CC KM=196 mM for (R,S)-1,2-propanediol {ECO:0000269|PubMed:15296184};
CC KM=49 mM for (R,S)-1,2-butanediol {ECO:0000269|PubMed:15296184};
CC KM=0.2 mM for 1,2-hexanediol {ECO:0000269|PubMed:7551050};
CC KM=1.4 mM for (R,S)-1,2-hexanediol {ECO:0000269|PubMed:15296184};
CC KM=0.5 mM for (R,S)-1,2,6-hexanetriol {ECO:0000269|PubMed:15296184};
CC KM=12 uM for NAD(+) (in the presence of 100 mM 1,2-hexanediol)
CC {ECO:0000269|PubMed:7551050};
CC KM=62 mM for acetoin {ECO:0000269|PubMed:7551050};
CC KM=144 mM for L-erythrulose {ECO:0000269|PubMed:7551050};
CC KM=202 mM for hydroxyacetone {ECO:0000269|PubMed:15296184};
CC KM=48 mM for dihydroxyacetone {ECO:0000269|PubMed:7551050};
CC KM=26 mM for 1-hydroxy-2-butanone {ECO:0000269|PubMed:15296184};
CC KM=1.4 mM for 2,3-hexanedione {ECO:0000269|PubMed:15296184};
CC KM=4.2 mM for 3,4-hexanedione {ECO:0000269|PubMed:15296184};
CC KM=4 uM for NADH (in the presence of 300 mM acetoin)
CC {ECO:0000269|PubMed:7551050};
CC pH dependence:
CC Optimum pH is 10.5 with 1,2-hexanediol as substrate. Optimum pH is
CC 4.0 with acetoin as substrate. {ECO:0000269|PubMed:7551050};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20410293,
CC ECO:0000269|PubMed:7551050}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:7551050}.
CC -!- BIOTECHNOLOGY: The wide substrate spectrum and the stereoselective mode
CC of action make GDH a very interesting enzyme for the production of
CC optically pure building blocks in the chemical synthesis of bioactive
CC compounds (PubMed:15296184). GDH could be covalently immobilized via
CC thiol bonds onto the surface of a gold electrode, which represents a
CC proof-of-concept for the development of reactors for electrochemical
CC synthon preparation using dehydrogenases (PubMed:19778027).
CC {ECO:0000269|PubMed:15296184, ECO:0000269|PubMed:19778027}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; FJ627003; ACM89305.1; -; Genomic_DNA.
DR EMBL; FJ627004; ACM89307.1; -; Genomic_DNA.
DR PDB; 2WDZ; X-ray; 1.95 A; A/B/C/D=1-254.
DR PDB; 2WSB; X-ray; 1.25 A; A/B/C/D=1-254.
DR PDB; 3LQF; X-ray; 1.80 A; A/B/C/D=1-254.
DR PDBsum; 2WDZ; -.
DR PDBsum; 2WSB; -.
DR PDBsum; 3LQF; -.
DR SMR; C0KTJ6; -.
DR BRENDA; 1.1.1.406; 5383.
DR EvolutionaryTrace; C0KTJ6; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..254
FT /note="Galactitol 2-dehydrogenase (L-tagatose-forming)"
FT /id="PRO_0000454239"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20410293"
FT BINDING 21..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 66..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20410293,
FT ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB,
FT ECO:0007744|PDB:3LQF"
FT TURN 3..7
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2WSB"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3LQF"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 157..177
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2WDZ"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2WSB"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2WSB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2WSB"
SQ SEQUENCE 254 AA; 26385 MW; 4DE97EFE965A7468 CRC64;
MDYRTVFRLD GACAAVTGAG SGIGLEICRA FAASGARLIL IDREAAALDR AAQELGAAVA
ARIVADVTDA EAMTAAAAEA EAVAPVSILV NSAGIARLHD ALETDDATWR QVMAVNVDGM
FWASRAFGRA MVARGAGAIV NLGSMSGTIV NRPQFASSYM ASKGAVHQLT RALAAEWAGR
GVRVNALAPG YVATEMTLKM RERPELFETW LDMTPMGRCG EPSEIAAAAL FLASPAASYV
TGAILAVDGG YTVW
