Reviewed, UniProtKB/Swiss-Prot P39633 (DHE2_BACSU)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + 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	Complete proteome
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro glutamate 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 – 424	424	NAD-specific glutamate dehydrogenase		PRO_0000182735
Sites
	Active site	116	1	By similarity
Experimental info
	Sequence conflict	324	1	R → A in BAD69594. Ref.2
	Sequence conflict	419 – 424	6	RFRGWV → FPRMGLI in CAA51631. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39633-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: DFE311C72BEA8091	FASTA	424	46,638
	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 VVERANGPTT 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]	"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.
[5]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X73124 Genomic DNA. Translation: CAA51631.1. AB194695 Genomic DNA. Translation: BAD69594.1. Z99123 Genomic DNA. Translation: CAB15806.1. S79622 Genomic DNA. No translation available.
PIR	A70055.
RefSeq	NP_391659.1.
3D structure databases
HSSP	HSSP built from PDB template 1GTM based on UniProtKB P80319.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39633.
Genome annotation databases
GeneID	937066.
GenomeReviews	Gene locus BSU37790 in contig AL009126_GR.
KEGG	bsu:BSU37790.
NMPDR	fig|224308.1.peg.3785.
Organism-specific databases
SubtiList	BG10621. rocG. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P39633.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3776-MON.
Family and domain databases
InterPro	IPR006095. Glu/Leu/Phe/Val_DHase. IPR006096. Glu/Leu/Phe/Val_DHase_C. IPR006097. Glu/Leu/Phe/Val_DHase_dimer. IPR014362. Glu_DHase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11606:SF2. GLFV_DH. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PIRSF	PIRSF000185. Glu_DH. 1 hit.
PRINTS	PR00082. GLFDHDRGNASE.
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:	December 15, 1998
Last modified:	November 25, 2008
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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