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.
CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + NADP⁺ = L-glutamyl 5-phosphate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000494; ABQ32705.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001236611.1; -.

3D structure databases

ModBase

A5E961.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004350;	Molecular function: glutamate-5-semialdehyde dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561;	Biological process: proline biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00412; -; 1.
PBIL [Tree]

InterPro

IPR016162; Ald_DHase_N.
IPR000965; Gglut_pp_reduct.
IPR012134; Glu-5-SA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11063:SF1; GSA_DH; 1.

PIRSF000151; GPR; 1.

TIGR00407; proA; 1.

PS01223; PROA; 1.

Genome annotation databases

GeneID

5155258; -.

GenomeReviews

CP000494_GR; BBta_0419.

KEGG

bbt:BBta_0419; -.

CMR

A5E961; BBta_0419.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Proline biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 429`	`429`		`Gamma-glutamyl phosphate reductase.`	`PRO_1000049937`

Sequence information

Length: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 44873 Da [This is the MW of the unprocessed precursor]

CRC64: B44F092B9EA27EE3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAPLKAIDG SADLPALMND LASRARAAAR VLALAPAAQK NRALEAMERL IRARVDTIIA 

        70         80         90        100        110        120 
ANAEDVVEAK AAGITSSFLD RLTLTPARVA AMADGIAAVR EVADPIGIVT ESWQRPNGMT 

       130        140        150        160        170        180 
IERVRVPLGV IGVIFESRPN VAADAGVLCL KSGNAVILRG GSDSFRSCRA IHECLVEGLR 

       190        200        210        220        230        240 
EAGLPDAAIT LVPTRDRAAV GLLLSGLNGG VDVIVPRGGK NLVARVEAEA RVPVFAHLEG 

       250        260        270        280        290        300 
VNHVYVDGAA DLEMAKSIVL NAKMRRTGVC GAAETLLIDR ASQDKIKPLV DTLINAGCEV 

       310        320        330        340        350        360 
RGDDAVRAAD ARVKPASNED WDTEYLDAVI AAKVVDGVEG AIAHIQAHGS HHTDAIVTAD 

       370        380        390        400        410        420 
VAAADKFLNE VDSAIVLHNA STQFADGGEF GFGAEIGIAT GKFHARGPVG VEQLTSFKYR 


IHGTGQTRP

A5E961 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools