A3PQJ2 (PROA_RHOS1) 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:	Rsph17029_3516

Organism

Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]

Taxonomic identifier

349101 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	420 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 – 420	420	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_1000049991

Sequences

	Sequence		Length	Mass (Da)
	A3PQJ2 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: E82DB68D72B7FDBD	FASTA	420	44,686
	10 20 30 40 50 60 MDGTDVTMLM REIGVRARAA AAELAFAEPS RKEEALNAAA EAMLARSDEI LEANGRDLAF 70 80 90 100 110 120 GAEKGLTPAM MDRLKLDAAR IDGIVEGLRA VAGQPDPVGQ VIAEWDRPSG LHIRRVRTPL 130 140 150 160 170 180 GVVGVIYESR PNVTADAGAL CLKSGNAVIL RGGSESFHSS GAIHAALQDG LRQAGLPVDA 190 200 210 220 230 240 IQRVPTRDRA AVAEMLRMVE HIDVIVPRGG KGLVGLVQAE ARVPVFAHLE GICHVYADGD 250 260 270 280 290 300 ADLEKARRVV LNAKTRRTGI CGSAECLLID RAFLAKHGPV LIEDLLKAGV EVRAEGELAQ 310 320 330 340 350 360 VPGTVPAQPE DFGREFLDMI IAAKVVDGVD EAIAHIRRYG SSHTESILTE NDATAERFFR 370 380 390 400 410 420 RLDSAILMRN ASTQFADGGE FGMGAEIGIA TGKMHARGPV GAEQLTSFKY LVTGDGTIRA

References

[1]

"Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC 17029." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000578 Genomic DNA. Translation: ABN78608.1.
RefSeq	YP_001045380.1. NC_009050.1.
3D structure databases
ProteinModelPortal	A3PQJ2.
ModBase	Search...
Protein-protein interaction databases
STRING	A3PQJ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4899177.
GenomeReviews	Gene locus Rsph17029_3516 in contig CP000578_GR.
KEGG	rsh:Rsph17029_3516.
PATRIC	23175005. VBIRhoSph114483_3777.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0014.
HOGENOM	HBG318080.
OMA	YGICGAM.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	RSPH349101:RSPH17029_3516-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_RHOS1

Accession

Primary (citable) accession number: A3PQJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	December 14, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program