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Protein

D-2-hydroxyisocaproate dehydrogenase

Gene
N/A
Organism
Lactobacillus paracasei
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD dependent reversible, stereospecific interconversion between 2-ketocarboxylic acids and D-2-hydroxy-carboxylic acids.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751NADCombined sources1 Publication
Binding sitei205 – 2051NAD; via carbonyl oxygenCombined sources1 Publication
Binding sitei211 – 2111NADCombined sources1 Publication
Active sitei234 – 2341By similarity
Binding sitei258 – 2581NADCombined sources1 Publication
Active sitei263 – 2631By similarity
Active sitei295 – 2951Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi155 – 1562NADCombined sources1 Publication
Nucleotide bindingi205 – 2062NADBy similarity
Nucleotide bindingi232 – 2343NADCombined sources1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
D-2-hydroxyisocaproate dehydrogenase (EC:1.1.1.-)
Short name:
D-HICDH
OrganismiLactobacillus paracasei
Taxonomic identifieri1597 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333D-2-hydroxyisocaproate dehydrogenasePRO_0000075940Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Turni10 – 123Combined sources
Helixi13 – 2311Combined sources
Beta strandi26 – 294Combined sources
Helixi38 – 425Combined sources
Beta strandi46 – 505Combined sources
Helixi58 – 669Combined sources
Beta strandi71 – 777Combined sources
Helixi84 – 896Combined sources
Beta strandi93 – 953Combined sources
Helixi102 – 11716Combined sources
Helixi120 – 1289Combined sources
Helixi132 – 1354Combined sources
Helixi143 – 1453Combined sources
Beta strandi146 – 1516Combined sources
Helixi155 – 16612Combined sources
Beta strandi170 – 1745Combined sources
Helixi191 – 1977Combined sources
Beta strandi199 – 2035Combined sources
Helixi209 – 2113Combined sources
Helixi217 – 2226Combined sources
Beta strandi227 – 2315Combined sources
Helixi240 – 2489Combined sources
Beta strandi251 – 2599Combined sources
Helixi263 – 27311Combined sources
Helixi279 – 2857Combined sources
Beta strandi290 – 2923Combined sources
Helixi301 – 32121Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXYX-ray1.86A1-333[»]
ProteinModelPortaliP17584.
SMRiP17584. Positions 1-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17584.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIIAYGARV DEIQYFKQWA KDTGNTLEYH TEFLDENTVE WAKGFDGINS
60 70 80 90 100
LQTTPYAAGV FEKMHAYGIK FLTIRNVGTD NIDMTAMKQY GIRLSNVPAY
110 120 130 140 150
SPAAIAEFAL TDTLYLLRNM GKVQAQLQAG DYEKAGTFIG KELGQQTVGV
160 170 180 190 200
MGTGHIGQVA IKLFKGFGAK VIAYDPYPMK GDHPDFDYVS LEDLFKQSDV
210 220 230 240 250
IDLHVPGIEQ NTHIINEAAF NLMKPGAIVI NTARPNLIDT QAMLSNLKSG
260 270 280 290 300
KLAGVGIDTY EYETEDLLNL AKHGSFKDPL WDELLGMPNV VLSPHIAYYT
310 320 330
ETAVHNMVYF SLQHLVDFLT KGETSTEVTG PAK
Length:333
Mass (Da):36,893
Last modified:November 1, 1997 - v2
Checksum:i40C165872884328B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 33312GETST…TGPAK → FKPARKLLVQQVVN (PubMed:2504649).CuratedAdd
BLAST

Mass spectrometryi

Molecular mass is 36880 Da from positions 1 - 333. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26929 Genomic DNA. Translation: AAA25236.1.
PIRiJU0050. DELBC.
RefSeqiWP_003577354.1. NZ_JVNI01000046.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26929 Genomic DNA. Translation: AAA25236.1.
PIRiJU0050. DELBC.
RefSeqiWP_003577354.1. NZ_JVNI01000046.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXYX-ray1.86A1-333[»]
ProteinModelPortaliP17584.
SMRiP17584. Positions 1-330.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP17584.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHD2_LACPA
AccessioniPrimary (citable) accession number: P17584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Can be applied in an industrial process for the production of D-amino acid.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.