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

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Cross-references

Sequence databases

EMBL

CP000124; ABA48649.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_334818.1; -.

3D structure databases

ModBase

Q3JNN5.

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: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

IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR000965; Gglut_pp_reduct.
IPR012134; Glu-5-SA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11063:SF1; GSA_DH; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PIRSF000151; GPR; 1.

TIGR00407; proA; 1.

PS01223; PROA; 1.

Genome annotation databases

GeneID

3691942; -.

GenomeReviews

CP000124_GR; BURPS1710b_3447.

KEGG

bpm:BURPS1710b_3447; -.

TIGR

BURPS1710b_3447; -.

Phylogenomic databases

HOGENOM

Q3JNN5; -.

Other

ProtoNet

Q3JNN5.

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`	`1 423`	`423`		`Gamma-glutamyl phosphate reductase.`	`PRO_0000229994`

Sequence information

Length: 423 AA [This is the length of the unprocessed precursor]

Molecular weight: 45106 Da [This is the MW of the unprocessed precursor]

CRC64: 6C80A878C798A1FA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDIDQYMTDV GRRARRASRE IARASTAAKN AALEAVARAI GRDADALKAA NARDVARAKD 

        70         80         90        100        110        120 
KGHDAAFVDR LTLSDKALKT MIEGLRQVAT LADPIGEMSN LKYRPSGIQV GQMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLAA AGLSQDAVQV 

       190        200        210        220        230        240 
VGTADRAAVG KLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRASV 

       250        260        270        280        290        300 
AKALAVCDNA KTHRYGTCNT METLLVARGI APAVLTPLGR LYREKGVELR VDADARAVLE 

       310        320        330        340        350        360 
AAGVGPLVDA TDEDWRTEYL APVLAIKIVD GIDAAIEHIN EYGSHHTDAI VTEDHDRAMR 

       370        380        390        400        410        420 
FLREVDSASV MVNASTRFAD GFEFGLGAEI GISNDKLHAR GPVGLEGLTS LKYVVLGHGE 


GRE

Q3JNN5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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