P39633 (DHE2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD-specific glutamate dehydrogenase
Short name=NAD-GDH
EC=1.4.1.2

Gene names

Name:	rocG
Synonyms:	yweB
Ordered Locus Names:	BSU37790
ORF Names:	ipa-75d

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catabolic GlutDH involved in the utilization of glutamate and other amino acids of the glutamate family.
Catalytic activity	L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.
Induction	By arginine, ornithine or proline.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	glutamate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gltC	P20668	2	EBI-1642022,EBI-1642006

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

NAD-specific glutamate dehydrogenase

PRO_0000182735

Sites

Active site

116

1

By similarity

Experimental info

Sequence conflict

324

1

A → R in CAA51631. Ref.1

Sequence conflict

419 – 424

6

RFRGWV → FPRMGLI in CAA51631. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

424

Helix Strand Turn

Details...

Helix

8 – 31

24

Helix

38 – 42

5

Beta strand

46 – 51

6

Beta strand

53 – 56

4

Beta strand

62 – 65

4

Beta strand

69 – 71

3

Helix

91 – 104

14

Helix

123 – 125

3

Helix

131 – 135

5

Helix

139 – 142

4

Helix

143 – 145

3

Helix

161 – 175

15

Turn

197 – 201

5

Helix

205 – 214

10

Helix

219 – 221

3

Beta strand

223 – 227

5

Helix

235 – 242

8

Helix

265 – 271

7

Helix

279 – 281

3

Helix

288 – 293

6

Beta strand

297 – 301

5

Turn

310 – 312

3

Helix

313 – 315

3

Beta strand

319 – 322

4

Helix

331 – 339

9

Beta strand

343 – 345

3

Helix

347 – 350

4

Helix

356 – 366

11

Helix

373 – 398

26

Helix

402 – 408

7

Helix

412 – 420

9

Sequences

	Sequence		Length	Mass (Da)
	P39633 [UniParc]. Last modified July 28, 2009. Version 3. Checksum: 019AE0A833BE48DD	FASTA	424	46,553
	10 20 30 40 50 60 MSAKQVSKDE EKEALNLFLS TQTIIKEALR KLGYPGDMYE LMKEPQRMLT VRIPVKMDNG 70 80 90 100 110 120 SVKVFTGYRS QHNDAVGPTK GGVRFHPEVN EEEVKALSIW MTLKCGIANL PYGGGKGGII 130 140 150 160 170 180 CDPRTMSFGE LERLSRGYVR AISQIVGPTK DIPAPDVYTN SQIMAWMMDE YSRLREFDSP 190 200 210 220 230 240 GFITGKPLVL GGSQGRETAT AQGVTICIEE AVKKKGIKLQ NARIIIQGFG NAGSFLAKFM 250 260 270 280 290 300 HDAGAKVIGI SDANGGLYNP DGLDIPYLLD KRDSFGMVTN LFTDVITNEE LLEKDCDILV 310 320 330 340 350 360 PAAISNQITA KNAHNIQASI VVEAANGPTT IDATKILNER GVLLVPDILA SAGGVTVSYF 370 380 390 400 410 420 EWVQNNQGYY WSEEEVAEKL RSVMVSSFET IYQTAATHKV DMRLAAYMTG IRKSAEASRF RGWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees." Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A. Mol. Microbiol. 10:371-384(1993) [PubMed: 7934828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Low thermostability of the NAD+ specific glutamate dehydrogenase from Bacillus subtilis ISW1214: cloning, purification and characterization." Khan M.H., Itoh K., Kim H., Ashida H., Ishikawa T., Shibata H., Sawa Y. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ISW1214.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 324.
[5]	"A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism." Klingel U., Miller C.M., North A.K., Stockley P.G., Baumberg S. Mol. Gen. Genet. 248:329-340(1995) [PubMed: 7565595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-424.
[6]	"Role and regulation of Bacillus subtilis glutamate dehydrogenase genes." Belitsky B.R., Sonenshein A.L. J. Bacteriol. 180:6298-6305(1998) [PubMed: 9829940] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73124 Genomic DNA. Translation: CAA51631.1.
AB194695 Genomic DNA. Translation: BAD69594.1.
AL009126 Genomic DNA. Translation: CAB15806.2.
S79622 Genomic DNA. No translation available.

PIR

A70055.

RefSeq

NP_391659.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3K92	X-ray	2.30	A/B/C/D/E/F	1-424	[»]

ProteinModelPortal

P39633.

SMR

P39633. Positions 7-424.

ModBase

Search...

Protein-protein interaction databases

IntAct

P39633. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000001904; EBBACP00000001904; EBBACG00000001901.

GeneID

937066.

GenomeReviews

Gene locus BSU37790 in contig AL009126_GR.

KEGG

bsu:BSU37790.

NMPDR

fig|224308.1.peg.3785.

PATRIC

18979598. VBIBacSub10457_3961.

Organism-specific databases

GenoList

BSU37790. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001222.

HOGENOM

HBG590661.

PhylomeDB

P39633.

ProtClustDB

CLSK888077.

Enzyme and pathway databases

BioCyc

BSUB:BSU37790-MONOMER.

Family and domain databases

InterPro

IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

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

KO

K00260.

Pfam

PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000185. Glu_DH. 1 hit.

PRINTS

PR00082. GLFDHDRGNASE.

SMART

SM00839. ELFV_dehydrog. 1 hit.
[Graphical view]

PROSITE

PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHE2_BACSU

Accession

Primary (citable) accession number: P39633
Secondary accession number(s): Q53548, Q5W7E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 28, 2009
Last modified:	January 25, 2012
This is version 86 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program