Q2S354 (PROA_SALRD) 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:	SRU_1253

Organism

Salinibacter ruber (strain DSM 13855 / M31)

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	436 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 Reference 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 – 436	436	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000252591

Sequences

	Sequence		Length	Mass (Da)
	Q2S354 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 5BE64AD5673581EE	FASTA	436	46,442
	10 20 30 40 50 60 MNKQINSVAP MSDTTSEALS VDALAADCKA AARELSTLST ETKNRTLRRM ADALEADEEA 70 80 90 100 110 120 ILAANGKDVS AAREEGLDDA LIDRLVLNPD RITKMADALR DVASFADPVG EMGGTTKRPS 130 140 150 160 170 180 GIEVGKMRIP LGVIGMIYEA RPNVTADAAG LCFKAGNAVL LRGGSNAFHS NQAVAAALHT 190 200 210 220 230 240 ALEAEGVPPA AVTLIPTTDR AAVQEMLTLN QHLDLIIPRG GEGLIRFVDE TSQIPVIKHY 250 260 270 280 290 300 KGVCHLYVDE DADLEVAEDL LLDGKVSRPS VCNALETLLV HADVADDFLP RARALLDDAG 310 320 330 340 350 360 VELRGDDRTR QLLPGVGAAT EDDYAAEYLD LTLAARVVES DDEALNHIAE YGSNHTEVIV 370 380 390 400 410 420 TDRLPTARRF VRSVDASVVL VNASSRFSDG GELGLGAEIG ISTTKLHAYG PMGLEALTTE 430 KFVVYGEGET RHPVEK

References

[1]

"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea." Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F. Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13855 / M31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000159 Genomic DNA. Translation: ABC43824.1.
RefSeq	YP_445377.1. NC_007677.1.
3D structure databases
HSSP	HSSP built from PDB template 2H5G based on UniProtKB P54886.
ProteinModelPortal	Q2S354.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2S354.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3851520.
GenomeReviews	Gene locus SRU_1253 in contig CP000159_GR.
KEGG	sru:SRU_1253.
NMPDR	fig|309807.5.peg.1171.
PATRIC	23424919. VBISalRub86502_1299.
TIGR	SRU_1253.
Phylogenomic databases
eggNOG	COG0014.
HOGENOM	HBG318080.
OMA	YGICGAM.
PhylomeDB	Q2S354.
ProtClustDB	CLSK2773663.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_1253-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. 2 hits.
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_SALRD

Accession

Primary (citable) accession number: Q2S354

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program