P17584 (DHD2_LACPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: D-2-hydroxyisocaproate dehydrogenase Short name=D-HICDH EC=1.1.1.-
Organism	Lactobacillus paracasei
Taxonomic identifier	1597 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NAD dependent reversible, stereospecific interconversion between 2-ketocarboxylic acids and D-2-hydroxy-carboxylic acids.
Subunit structure	Homodimer.
Miscellaneous	Can be applied in an industrial process for the production of D-amino acid.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Mass spectrometry	Molecular mass is 36880 Da from positions 1 - 333. Determined by ESI. Ref.2

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

D-2-hydroxyisocaproate dehydrogenase

PRO_0000075940

Regions

Nucleotide binding

155 – 156

2

NAD By similarity

Nucleotide binding

232 – 234

3

NAD By similarity

Nucleotide binding

295 – 298

4

NAD By similarity

Sites

Active site

234

1

Active site

263

1

Active site

295

1

Proton donor

Binding site

258

1

NAD By similarity

Experimental info

Sequence conflict

322 – 333

12

GETST…TGPAK → FKPARKLLVQQVVN Ref.1

Secondary structure

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333

Helix Strand Turn

Details...

Beta strand

2 – 5

4

Turn

10 – 12

3

Helix

13 – 23

11

Beta strand

26 – 29

4

Helix

38 – 42

5

Beta strand

46 – 50

5

Helix

58 – 66

9

Beta strand

71 – 77

7

Helix

84 – 89

6

Beta strand

93 – 95

3

Helix

102 – 117

16

Helix

120 – 128

9

Helix

132 – 135

4

Helix

143 – 145

3

Beta strand

146 – 151

6

Helix

155 – 166

12

Beta strand

170 – 174

5

Helix

191 – 197

7

Beta strand

199 – 203

5

Helix

209 – 211

3

Helix

217 – 222

6

Beta strand

227 – 231

5

Helix

240 – 248

9

Beta strand

251 – 259

9

Helix

263 – 273

11

Helix

279 – 285

7

Beta strand

290 – 292

3

Helix

301 – 321

21

Sequences

	Sequence		Length	Mass (Da)
	P17584 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 40C165872884328B	FASTA	333	36,893
	10 20 30 40 50 60 MKIIAYGARV DEIQYFKQWA KDTGNTLEYH TEFLDENTVE WAKGFDGINS LQTTPYAAGV 70 80 90 100 110 120 FEKMHAYGIK FLTIRNVGTD NIDMTAMKQY GIRLSNVPAY SPAAIAEFAL TDTLYLLRNM 130 140 150 160 170 180 GKVQAQLQAG DYEKAGTFIG KELGQQTVGV MGTGHIGQVA IKLFKGFGAK VIAYDPYPMK 190 200 210 220 230 240 GDHPDFDYVS LEDLFKQSDV IDLHVPGIEQ NTHIINEAAF NLMKPGAIVI NTARPNLIDT 250 260 270 280 290 300 QAMLSNLKSG KLAGVGIDTY EYETEDLLNL AKHGSFKDPL WDELLGMPNV VLSPHIAYYT 310 320 330 ETAVHNMVYF SLQHLVDFLT KGETSTEVTG PAK

References

[1]	"Cloning, sequencing and expression in Escherichia coli of the D-2-hydroxyisocaproate dehydrogenase gene of Lactobacillus casei." Lerch H.-P., Bloecker H., Kallwass H., Hoppe J., Tsai H., Collins J. Gene 78:47-57(1989) [PubMed: 2504649] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 25598 / DSM 20008 / JCM 1181 / NCDO 2743 / NCIMB 9713.
[2]	"Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9-A resolution." Dengler U., Niefind K., Kiess M., Schomburg D. J. Mol. Biol. 267:640-660(1997) [PubMed: 9126843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION TO 322-333, MASS SPECTROMETRY. Strain: ATCC 25598 / DSM 20008 / JCM 1181 / NCDO 2743 / NCIMB 9713.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M26929 Genomic DNA. Translation: AAA25236.1.

PIR

DELBC. JU0050.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DXY	X-ray	1.86	A	1-333	[»]

ProteinModelPortal

P17584.

SMR

P17584. Positions 1-330.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.

Pfam

PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]

PROSITE

PS00065. 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]

ProtoNet

Search...

Entry information

Entry name

DHD2_LACPA

Accession

Primary (citable) accession number: P17584

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 1, 1997
Last modified:	June 28, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program