A2BVQ3 (PROA_PROM5) 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:	P9515_06551

Organism

Prochlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]

Taxonomic identifier

167542 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

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
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_1000049979

Sequences

	Sequence		Length	Mass (Da)
	A2BVQ3 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: F160ECB82A5E8638	FASTA	436	47,921
	10 20 30 40 50 60 MTDIFEVPSP DNNLLDKAEQ LRLASIKTSQ TNNNERIRAL NLMADSLEKN SKEIIDSNFE 70 80 90 100 110 120 DYKKAEIKGI SKALLSRLKL SKEKLNLGIE GIRKVGDLSD PLGQIQIKKE LSKGLILERK 130 140 150 160 170 180 TVPIGVLGVI FESRPDAVMQ ISSLAIRAGN GVMLKGGSEA NFTNQAIVSA LKKGLQKSNI 190 200 210 220 230 240 DDNAICLLTS RKDSMAMLNL EKFINLIIPR GSNELVKFIQ ENTGIPVLGH ADGICHLYID 250 260 270 280 290 300 DEVNLDIALK VALDSKIQYP AACNAIETLL IHKSIAPAFL KKAIPIFNSN NVKLIGDKKA 310 320 330 340 350 360 VKLGVAFEAN YEDWQTEYLD LILSIKIVDD LEEGIAHIQK FSSKHTDGII TENISNANKF 370 380 390 400 410 420 MSEIDSAGVF HNCSTRFADG FRYGFGAEVG ISTQTLPPRG PVGLEGLVTY KYFLRGEGHS 430 VDDFSSGKSI YTHKDL

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9515.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000552 Genomic DNA. Translation: ABM71864.1.
RefSeq	YP_001010971.1. NC_008817.1.
3D structure databases
ProteinModelPortal	A2BVQ3.
ModBase	Search...
Protein-protein interaction databases
STRING	A2BVQ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4719664.
GenomeReviews	Gene locus P9515_06551 in contig CP000552_GR.
KEGG	pmc:P9515_06551.
PATRIC	23014892. VBIProMar113831_0674.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0014.
HOGENOM	HBG318080.
OMA	QYPAACN.
PhylomeDB	A2BVQ3.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	PMAR167542:P9515ORF_0691-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. 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.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_PROM5

Accession

Primary (citable) accession number: A2BVQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 20, 2007
Last modified:	December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program