Q8FN87 (PROA_COREF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-glutamyl phosphate reductase
Short name=GPR
EC=1.2.1.41

Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Short name=GSA dehydrogenase

Gene names

Name:	proA
Ordered Locus Names:	CE2260

Organism

Corynebacterium efficiens [Complete proteome] [HAMAP]

Taxonomic identifier

152794 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. HAMAP MF_00412
Catalytic activity	L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412
Subcellular location	Cytoplasm By similarity HAMAP MF_00412.
Sequence similarities	Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde 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 – 438	438	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189718

Sequences

	Sequence		Length	Mass (Da)
	Q8FN87 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C0C2D1825A9808C0	FASTA	438	46,362
	10 20 30 40 50 60 MTAQTSSDVT DQKTDLTRES ERDEVLAKAT LAKKVAPEIA QLGTGVKNQI LLAAAEALLE 70 80 90 100 110 120 RSAEIIEANS RDIAAGRESG MAESLIDRLA LDEGRIEGIA GGLRQVAGLT DPVGEVLQGR 130 140 150 160 170 180 VMENGIQMRQ VRVPLGVMGM VYEARPNVTV DAFGLALKSG NVALLRGSST AVHSNTTLVG 190 200 210 220 230 240 ILQDVLATFD LPRETVQLLP CATRESVQDL ITARGLVDVV IPRGGAGLIN AVVMGATVPT 250 260 270 280 290 300 IETGTGNCHF YIDGDVDVDS AIAMLINGKT RRCSVCNATE TALIDSALPD VDKLRVVRAL 310 320 330 340 350 360 QDAGVTVHGR VAELEAFGAT DVVEATENDW DSEYLSFDIA VAVVDGVDAA IEHIEKYSTH 370 380 390 400 410 420 HTEAIATNNV FTAQRFADHV DAAAVMINAS TAFTDGEQYG MGAEIGISTQ KLHARGPMAL 430 PELTSTKWIL QGTGHTRP

References

[1]

"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000035 Genomic DNA. Translation: BAC19070.1.
RefSeq	NP_738870.1. NC_004369.1.
3D structure databases
ProteinModelPortal	Q8FN87.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1032084.
GenomeReviews	Gene locus CE2260 in contig BA000035_GR.
KEGG	cef:CE2260.
NMPDR	fig|196164.1.peg.2260.
PATRIC	21490647. VBICorEff9312_2235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG318080.
OMA	QYPAACN.
PhylomeDB	Q8FN87.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	CEFF196164:CE2260-MONOMER.
Family and domain databases
HAMAP	MF_00412. ProA. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR000965. G-glutamylP_reductase. IPR020593. G-glutamylP_reductase_CS. IPR012134. Glu-5-SA_DH. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K00147.
PANTHER	PTHR11063:SF1. GSA_DH. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF000151. GPR. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00407. ProA. 1 hit.
PROSITE	PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_COREF

Accession

Primary (citable) accession number: Q8FN87

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program