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Database: UniProt
Entry: Q2VEQ7
LinkDB: Q2VEQ7
Original site: Q2VEQ7 
ID   DDH_HALMT               Reviewed;         308 AA.
AC   Q2VEQ7; I3R656;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=D-2-hydroxyacid dehydrogenase;
DE            Short=D2-HDH;
DE            EC=1.1.1.-;
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
GN   Name=ddh; Synonyms=serA5; OrderedLocusNames=HFX_2024;
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   KINETIC PARAMETERS, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4;
RX   PubMed=17049749; DOI=10.1016/j.bbagen.2006.08.024;
RA   Domenech J., Ferrer J.;
RT   "A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity
RT   from Haloferax mediterranei, sequence analysis and heterologous
RT   overexpression.";
RL   Biochim. Biophys. Acta 1760:1667-1674(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4;
RX   PubMed=22843593; DOI=10.1128/JB.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
RA   Chen Y., Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
CC   -!- FUNCTION: Catalyzes the stereospecific NAD(P)H-dependent reduction
CC       of 2-ketocarboxylic acids into the corresponding D-2-
CC       hydroxycarboxylic acids. Can use both NADPH or NADH as reductant,
CC       displaying a marked preference for NADPH over NADH. Shows a broad
CC       substrate specificity, although it displays a marked preference
CC       for the 2-ketocarboxylic acids having an unbranched chain of 4-5
CC       carbon atoms. {ECO:0000269|PubMed:17049749}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.31 mM for 2-ketoisoleucine (in the presence of NADPH, at pH
CC         8.5 and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=11.9 mM for 2-ketoisoleucine (in the presence of NADH, at pH
CC         8.5 and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=3.77 mM for 2-ketoisocaproate (in the presence of NADPH, at
CC         pH 8.5 and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=13.9 mM for 2-ketoisocaproate (in the presence of NADH, at pH
CC         8.5 and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=13.45 mM for 2-ketobutyrate (in the presence of NADPH, at pH
CC         8.5 and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=106 mM for 2-ketobutyrate (in the presence of NADH, at pH 8.5
CC         and 40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=21.96 mM for pyruvate (in the presence of NADPH, at pH 5 and
CC         40 degrees Celsius) {ECO:0000269|PubMed:17049749};
CC         KM=0.046 mM for NADPH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         KM=0.33 mM for NADH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=1.733 umol/min/mg enzyme for the reduction of 2-
CC         ketoisoleucine by NADPH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=1.02 umol/min/mg enzyme for the reduction of 2-
CC         ketoisoleucine by NADH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=1.47 umol/min/mg enzyme for the reduction of 2-
CC         ketoisocaproate by NADPH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=0.94 umol/min/mg enzyme for the reduction of 2-
CC         ketoisocaproate by NADH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=2.09 umol/min/mg enzyme for the reduction of 2-ketobutyrate
CC         by NADPH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=2.1 umol/min/mg enzyme for the reduction of 2-ketobutyrate
CC         by NADH (at pH 8.5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC         Vmax=0.8 umol/min/mg enzyme for the reduction of pyruvate by
CC         NADPH (at pH 5 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:17049749};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17049749}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; DQ223970; ABB30004.1; -; Genomic_DNA.
DR   EMBL; CP001868; AFK19716.1; -; Genomic_DNA.
DR   RefSeq; WP_004059362.1; NZ_CP007551.1.
DR   PDB; 5MH5; X-ray; 1.40 A; A/B=1-308.
DR   PDB; 5MH6; X-ray; 1.35 A; A/B/C/D=1-308.
DR   PDB; 5MHA; X-ray; 1.57 A; A/B=1-308.
DR   PDBsum; 5MH5; -.
DR   PDBsum; 5MH6; -.
DR   PDBsum; 5MHA; -.
DR   ProteinModelPortal; Q2VEQ7; -.
DR   SMR; Q2VEQ7; -.
DR   EnsemblBacteria; AFK19716; AFK19716; HFX_2024.
DR   GeneID; 13028184; -.
DR   KEGG; hme:HFX_2024; -.
DR   KO; K17064; -.
DR   OMA; YGAGVDH; -.
DR   OrthoDB; 36410at2157; -.
DR   BioCyc; HMED523841:G1HBL-2706-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-17694; -.
DR   BRENDA; 1.1.1.272; 2566.
DR   SABIO-RK; Q2VEQ7; -.
DR   Proteomes; UP000006469; Chromosome.
DR   GO; GO:0031406; F:carboxylic acid binding; IDA:UniProtKB.
DR   GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR   GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IDA:UniProtKB.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    308       D-2-hydroxyacid dehydrogenase.
FT                                /FTId=PRO_0000414497.
FT   NP_BIND     145    146       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     224    226       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     274    277       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    226    226       {ECO:0000250}.
FT   ACT_SITE    255    255       {ECO:0000250}.
FT   ACT_SITE    274    274       Proton donor. {ECO:0000250}.
FT   BINDING     250    250       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   STRAND        5      9       {ECO:0000244|PDB:5MH6}.
FT   HELIX        10     14       {ECO:0000244|PDB:5MH6}.
FT   HELIX        18     24       {ECO:0000244|PDB:5MH6}.
FT   TURN         25     27       {ECO:0000244|PDB:5MH6}.
FT   STRAND       28     30       {ECO:0000244|PDB:5MH6}.
FT   STRAND       32     35       {ECO:0000244|PDB:5MH6}.
FT   STRAND       45     51       {ECO:0000244|PDB:5MH6}.
FT   HELIX        54     58       {ECO:0000244|PDB:5MH6}.
FT   STRAND       59     67       {ECO:0000244|PDB:5MH6}.
FT   HELIX        74     80       {ECO:0000244|PDB:5MH6}.
FT   STRAND       83     85       {ECO:0000244|PDB:5MH6}.
FT   HELIX        92    108       {ECO:0000244|PDB:5MH6}.
FT   HELIX       110    118       {ECO:0000244|PDB:5MH6}.
FT   STRAND      137    141       {ECO:0000244|PDB:5MH6}.
FT   HELIX       145    156       {ECO:0000244|PDB:5MH6}.
FT   STRAND      160    164       {ECO:0000244|PDB:5MH6}.
FT   STRAND      175    178       {ECO:0000244|PDB:5MH6}.
FT   HELIX       180    182       {ECO:0000244|PDB:5MH6}.
FT   HELIX       183    187       {ECO:0000244|PDB:5MH6}.
FT   STRAND      191    195       {ECO:0000244|PDB:5MH6}.
FT   TURN        201    205       {ECO:0000244|PDB:5MH6}.
FT   HELIX       209    214       {ECO:0000244|PDB:5MH6}.
FT   STRAND      220    223       {ECO:0000244|PDB:5MH6}.
FT   HELIX       227    229       {ECO:0000244|PDB:5MH6}.
FT   HELIX       232    241       {ECO:0000244|PDB:5MH6}.
FT   STRAND      246    250       {ECO:0000244|PDB:5MH6}.
FT   STRAND      253    256       {ECO:0000244|PDB:5MH6}.
FT   HELIX       262    265       {ECO:0000244|PDB:5MH6}.
FT   STRAND      269    271       {ECO:0000244|PDB:5MH6}.
FT   HELIX       282    299       {ECO:0000244|PDB:5MH6}.
FT   STRAND      306    308       {ECO:0000244|PDB:5MHA}.
SQ   SEQUENCE   308 AA;  33336 MW;  20D4FB8CE01D64AA CRC64;
     MHIERLAVDE SVGRAMPPQR FIEALSDLGV PVEFAGEDEQ FGPGDAVASF GHRDAFLDAD
     WVHCIRAGYD EFPVGVYEEA GTYLTNSTGI HGTTVGETVA GYMLTFARRL HAYRDAQHDH
     AWDLPRYEEP FTLAGERVCV VGLGTLGRGV VDRAAALGME VVGVRRSGDP VDNVSTVYTP
     DRLHEAIADA RFVVLATPLT DETEGMVAAP EFETMREDAS LVNVARGPVV VESDLVAALD
     SGDIAGAALD VFSEEPLPED SPLWDFEDVL ITPHVSAATS KYHEDVAALI RENIEKIATG
     DELTNRVV
//
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