Reviewed, UniProtKB/Swiss-Prot Q44297 (ODH_ARTSC)

Names and origin

Protein names

Recommended name:
    Opine dehydrogenase
    EC=1.5.1.28
Alternative name(s):
    N-(1-D-carboxyethyl)-L-norvaline dehydrogenase

Gene names

Name:

odh

Organism

Arthrobacter sp. (strain 1C)

Taxonomic identifier

79670 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In the forward direction acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. In the reverse direction, the enzyme also acts on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.
Catalytic activity	(2S)-2-((1-(R)-carboxyethyl)amino)pentanoate + NAD(+) + H(2)O = L-2-aminopentanoic acid + pyruvate + NADH.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the lysopine/nopaline/octopine/opine/vitopine dehydrogenases family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: InterPro opine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Opine dehydrogenase

PRO_0000179982

Secondary structure

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359

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

14 – 25

12

Beta strand

29 – 33

5

Helix

37 – 46

10

Beta strand

48 – 55

8

Beta strand

58 – 60

3

Beta strand

63 – 67

5

Helix

69 – 73

5

Beta strand

77 – 81

5

Helix

85 – 87

3

Helix

88 – 95

8

Helix

96 – 98

3

Beta strand

104 – 109

6

Helix

114 – 124

11

Beta strand

131 – 137

7

Beta strand

139 – 143

5

Beta strand

149 – 155

7

Beta strand

159 – 165

7

Helix

166 – 168

3

Helix

169 – 176

8

Turn

177 – 179

3

Beta strand

183 – 185

3

Helix

189 – 194

6

Helix

197 – 201

5

Helix

203 – 207

5

Helix

210 – 214

5

Helix

221 – 225

5

Helix

228 – 246

19

Turn

247 – 249

3

Helix

255 – 258

4

Helix

270 – 275

6

Helix

278 – 280

3

Beta strand

287 – 289

3

Helix

292 – 299

8

Helix

302 – 311

10

Helix

317 – 329

13

Helix

334 – 337

4

Turn

341 – 345

5

Helix

351 – 358

8

Sequences

	Sequence		Length	Mass (Da)
	Q44297-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7542D8A44D859028	FASTA	359	37,937
	10 20 30 40 50 60 MIESKTYAVL GLGNGGHAFA AYLALKGQSV LAWDIDAQRI KEIQDRGAII AEGPGLAGTA 70 80 90 100 110 120 HPDLLTSDIG LAVKDADVIL IVVPAIHHAS IAANIASYIS EGQLIILNPG ATGGALEFRK 130 140 150 160 170 180 ILRENGAPEV TIGETSSMLF TCRSERPGQV TVNAIKGAMD FACLPAAKAG WALEQIGSVL 190 200 210 220 230 240 PQYVAVENVL HTSLTNVNAV MHPLPTLLNA ARCESGTPFQ YYLEGITPSV GSLAEKVDAE 250 260 270 280 290 300 RIAIAKAFDL NVPSVCEWYK ESYGQSPATI YEAVQGNPAY RGIAGPINLN TRYFFEDVST 310 320 330 340 350 GLVPLSELGR AVNVPTPLID AVLDLISSLI DTDFRKEGRT LEKLGLSGLT AAGIRSAVE

References

[1]	"Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C." Dairi T., Asano Y. Appl. Environ. Microbiol. 61:3169-3171(1995) [PubMed: 7487048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C." Asano Y., Yamaguchi K., Kondo K. J. Bacteriol. 171:4466-4471(1989) [PubMed: 2753861] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase." Britton K.L., Asano Y., Rice D.W. Nat. Struct. Biol. 5:593-601(1998) [PubMed: 9665174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

D45211 Genomic DNA. Translation: BAA08145.1.

PIR

I39664.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BG6	X-ray	1.80	A	1-359	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR013328. DHase_multihelical.
IPR016040. NAD(P)-bd.
IPR006168. NAD-dep_Gly3P_DHase.
IPR011128. NAD-dep_Gly3P_DHase_N.
IPR003421. Opine_DHase.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.

PANTHER

PTHR11728. NAD_Gly3P_DH. 1 hit.

Pfam

PF01210. NAD_Gly3P_dh_N. 1 hit.
PF02317. Octopine_DH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ODH_ARTSC

Accession

Primary (citable) accession number: Q44297

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)