UniProtKB - Q2VEQ7 (DDH_HALMT)
Protein
D-2-hydroxyacid dehydrogenase
Gene
ddh
Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Status
Functioni
Catalyzes the stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. Can use both NADPH or NADH as reductant, displaying a marked preference for NADPH over NADH. Shows a broad substrate specificity, although it displays a marked preference for the 2-ketocarboxylic acids having an unbranched chain of 4-5 carbon atoms.1 Publication
Kineticsi
- KM=1.31 mM for 2-ketoisoleucine (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=11.9 mM for 2-ketoisoleucine (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=3.77 mM for 2-ketoisocaproate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=13.9 mM for 2-ketoisocaproate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=13.45 mM for 2-ketobutyrate (in the presence of NADPH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=106 mM for 2-ketobutyrate (in the presence of NADH, at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=21.96 mM for pyruvate (in the presence of NADPH, at pH 5 and 40 degrees Celsius)1 Publication
- KM=0.046 mM for NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
- KM=0.33 mM for NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=1.733 µmol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=1.02 µmol/min/mg enzyme for the reduction of 2-ketoisoleucine by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=1.47 µmol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=0.94 µmol/min/mg enzyme for the reduction of 2-ketoisocaproate by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=2.09 µmol/min/mg enzyme for the reduction of 2-ketobutyrate by NADPH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=2.1 µmol/min/mg enzyme for the reduction of 2-ketobutyrate by NADH (at pH 8.5 and 40 degrees Celsius)1 Publication
- Vmax=0.8 µmol/min/mg enzyme for the reduction of pyruvate by NADPH (at pH 5 and 40 degrees Celsius)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 226 | By similarity | 1 | |
Binding sitei | 250 | NADBy similarity | 1 | |
Active sitei | 255 | By similarity | 1 | |
Active sitei | 274 | Proton donorBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 145 – 146 | NADBy similarity | 2 | |
Nucleotide bindingi | 224 – 226 | NADBy similarity | 3 | |
Nucleotide bindingi | 274 – 277 | NADBy similarity | 4 |
GO - Molecular functioni
- carboxylic acid binding Source: UniProtKB
- NADH binding Source: UniProtKB
- NADPH binding Source: UniProtKB
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: UniProtKB
GO - Biological processi
- carboxylic acid metabolic process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NAD, NADP |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-17694 |
BRENDAi | 1.1.1.272, 2566 |
SABIO-RKi | Q2VEQ7 |
Names & Taxonomyi
Protein namesi | Recommended name: D-2-hydroxyacid dehydrogenase (EC:1.1.1.-)Short name: D2-HDH Alternative name(s): D-specific 2-hydroxyacid dehydrogenase |
Gene namesi | Name:ddh Synonyms:serA5 Ordered Locus Names:HFX_2024 |
Organismi | Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei) |
Taxonomic identifieri | 523841 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Stenosarchaea group › Halobacteria › Haloferacales › Haloferacaceae › Haloferax › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000414497 | 1 – 308 | D-2-hydroxyacid dehydrogenaseAdd BLAST | 308 |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
STRINGi | 523841.HFX_2024 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q2VEQ7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | arCOG01757, Archaea |
HOGENOMi | CLU_019796_1_0_2 |
OMAi | HVAGWSP |
OrthoDBi | 36410at2157 |
Family and domain databases
InterProi | View protein in InterPro IPR006140, D-isomer_DH_NAD-bd IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF02826, 2-Hacid_dh_C, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
i Sequence
Sequence statusi: Complete.
Q2VEQ7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MHIERLAVDE SVGRAMPPQR FIEALSDLGV PVEFAGEDEQ FGPGDAVASF
60 70 80 90 100
GHRDAFLDAD WVHCIRAGYD EFPVGVYEEA GTYLTNSTGI HGTTVGETVA
110 120 130 140 150
GYMLTFARRL HAYRDAQHDH AWDLPRYEEP FTLAGERVCV VGLGTLGRGV
160 170 180 190 200
VDRAAALGME VVGVRRSGDP VDNVSTVYTP DRLHEAIADA RFVVLATPLT
210 220 230 240 250
DETEGMVAAP EFETMREDAS LVNVARGPVV VESDLVAALD SGDIAGAALD
260 270 280 290 300
VFSEEPLPED SPLWDFEDVL ITPHVSAATS KYHEDVAALI RENIEKIATG
DELTNRVV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ223970 Genomic DNA Translation: ABB30004.1 CP001868 Genomic DNA Translation: AFK19716.1 |
RefSeqi | WP_004059362.1, NZ_CP039139.1 |
Genome annotation databases
EnsemblBacteriai | AFK19716; AFK19716; HFX_2024 |
GeneIDi | 40155066 |
KEGGi | hme:HFX_2024 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ223970 Genomic DNA Translation: ABB30004.1 CP001868 Genomic DNA Translation: AFK19716.1 |
RefSeqi | WP_004059362.1, NZ_CP039139.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5MH5 | X-ray | 1.40 | A/B | 1-308 | [»] | |
5MH6 | X-ray | 1.35 | A/B/C/D | 1-308 | [»] | |
5MHA | X-ray | 1.57 | A/B | 1-308 | [»] | |
SMRi | Q2VEQ7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 523841.HFX_2024 |
Genome annotation databases
EnsemblBacteriai | AFK19716; AFK19716; HFX_2024 |
GeneIDi | 40155066 |
KEGGi | hme:HFX_2024 |
Phylogenomic databases
eggNOGi | arCOG01757, Archaea |
HOGENOMi | CLU_019796_1_0_2 |
OMAi | HVAGWSP |
OrthoDBi | 36410at2157 |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-17694 |
BRENDAi | 1.1.1.272, 2566 |
SABIO-RKi | Q2VEQ7 |
Family and domain databases
InterProi | View protein in InterPro IPR006140, D-isomer_DH_NAD-bd IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF02826, 2-Hacid_dh_C, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DDH_HALMT | |
Accessioni | Q2VEQ7Primary (citable) accession number: Q2VEQ7 Secondary accession number(s): I3R656 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 14, 2011 |
Last sequence update: | January 10, 2006 | |
Last modified: | December 2, 2020 | |
This is version 74 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families