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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)DescriptionActionsGraphical viewLength
Binding sitei175NADCombined sources1 Publication1
Binding sitei205NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei211NADCombined sources1 Publication1
Active sitei234By similarity1
Binding sitei258NADCombined sources1 Publication1
Active sitei263By similarity1
Active sitei295Proton donorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi155 – 156NADCombined sources1 Publication2
Nucleotide bindingi205 – 206NADBy similarity2
Nucleotide bindingi232 – 234NADCombined sources1 Publication3

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000759401 – 333D-2-hydroxyisocaproate dehydrogenaseAdd BLAST333

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Turni10 – 12Combined sources3
Helixi13 – 23Combined sources11
Beta strandi26 – 29Combined sources4
Helixi38 – 42Combined sources5
Beta strandi46 – 50Combined sources5
Helixi58 – 66Combined sources9
Beta strandi71 – 77Combined sources7
Helixi84 – 89Combined sources6
Beta strandi93 – 95Combined sources3
Helixi102 – 117Combined sources16
Helixi120 – 128Combined sources9
Helixi132 – 135Combined sources4
Helixi143 – 145Combined sources3
Beta strandi146 – 151Combined sources6
Helixi155 – 166Combined sources12
Beta strandi170 – 174Combined sources5
Helixi191 – 197Combined sources7
Beta strandi199 – 203Combined sources5
Helixi209 – 211Combined sources3
Helixi217 – 222Combined sources6
Beta strandi227 – 231Combined sources5
Helixi240 – 248Combined sources9
Beta strandi251 – 259Combined sources9
Helixi263 – 273Combined sources11
Helixi279 – 285Combined sources7
Beta strandi290 – 292Combined sources3
Helixi301 – 321Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXYX-ray1.86A1-333[»]
ProteinModelPortaliP17584.
SMRiP17584.
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)DescriptionActionsGraphical viewLength
Sequence conflicti322 – 333GETST…TGPAK → FKPARKLLVQQVVN (PubMed:2504649).CuratedAdd BLAST12

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXYX-ray1.86A1-333[»]
ProteinModelPortaliP17584.
SMRiP17584.
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: November 30, 2016
This is version 99 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.