Reviewed, UniProtKB/Swiss-Prot P28997 (DHE2_PEPAS)

Names and origin

Protein names	Recommended name:     NAD-specific glutamate dehydrogenase       Short name=NAD-GDH     EC=1.4.1.2
Organism	Peptostreptococcus asaccharolyticus (Peptococcus asaccharolyticus)
Taxonomic identifier	1258 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XI. Incertae Sedis › Peptoniphilus

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.
Pathway	Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 1/5.
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	cellular 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 – 421	421	NAD-specific glutamate dehydrogenase		PRO_0000182739
Sites
	Active site	106	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28997-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: DDA64241C027422C	FASTA	421	46,514
	10 20 30 40 50 60 MTDTLNPLVA AQEKVRIACE KLGCDPAVYE LLKEPQRVIE ISIPVKMDDG TVKVFKGWRS 70 80 90 100 110 120 AHSSAVGPSK GGVRFHPNVN MDEVKALSLW MTFKGGALGL PYGGGKGGIC VDPAELSERE 130 140 150 160 170 180 LEQLSRGWVR GLYKYLGDRI DIPAPDVNTN GQIMSWFVDE YVKLNGERMD IGTFTGKPVA 190 200 210 220 230 240 FGGSEGRNEA TGFGVAVVVR ESAKRFGIKM EDAKIAVQGF GNVGTFTVKN IERQGGKVCA 250 260 270 280 290 300 IAEWDRNEGN YALYNENGID FKELLAYKEA NKTLIGFPGA ERITDEEFWT KEYDIIVPAA 310 320 330 340 350 360 LENVITGERA KTINAKLVCE AANGPTTPEG DKVLTERGIN LTPDILTNSG GVLVSYYEWV 370 380 390 400 410 420 QNQYGYYWTE AEVEEKQEAD MMKAIKGVFA VADEYNVTLR EAVYMYAIKS IDVAMKLRGW Y

References

[1]	"Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus." Snedecor B., Chu H., Chen E.Y. J. Bacteriol. 173:6162-6167(1991) [PubMed: 1917850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M76403 Genomic DNA. Translation: AAA25611.1.
PIR	A38168.
3D structure databases
HSSP	HSSP built from PDB template 1EUZ based on UniProtKB O74024.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-1161.
BRENDA	1.4.1.2. 142947.
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. IPR014362. Glu_DH. IPR016040. NAD(P)-bd_dom. [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_PEPAS

Accession

Primary (citable) accession number: P28997

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	September 22, 2009
This is version 48 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)