[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Miller W.G., Rubenfield M., Wang G., Rogosin A., Malek J., Parker C.T., Stanker L.H., Mandrell R.E.; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.

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.
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

CP000361; ABV68003.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001490673.1; -.

3D structure databases

ModBase

A8EVN0.

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.
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.

PIRSF000151; GPR; 1.

TIGR00407; proA; 1.

PS01223; PROA; 1.

Genome annotation databases

GeneID

5624120; -.

GenomeReviews

CP000361_GR; Abu_1757.

KEGG

abu:Abu_1757; -.

CMR

A8EVN0; Abu_1757.

Other

ProtoNet

A8EVN0.

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`	`1 412`	`412`		`Gamma-glutamyl phosphate reductase.`	`PRO_1000060837`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 45081 Da [This is the MW of the unprocessed precursor]

CRC64: 1DB0933298630615 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQEFLQEAKN SSRIIANLGS AQKNRVLNEM ADALIEHSSF ILSHNQKDMN DAKLNNLNDA 

        70         80         90        100        110        120 
LQDRLLLTEK RIQDMAIAIR QIASQQDPLG KILNGWVTKD GLNIQKVSIP IGVIGIIYES 

       130        140        150        160        170        180 
RPNVTSDTAA LCFKSGNVCV LKGGKEAENS NKAIATILRE VLRKNNLPEY AISLLPDSSR 

       190        200        210        220        230        240 
EGVAKLIKQD KYVDLIVPRG GEALIRFVSE NSSIPVIKHD KGICHIFIDQ DANITKIFDI 

       250        260        270        280        290        300 
VVNAKCQKPS ACNSIETLLI HTNIAALILS GLVETLSLHG TILKGCPETL QHINAIPATL 

       310        320        330        340        350        360 
EDFDTEYLAN VLNIKIVANV DEAITHIQRH GSGHSESILS ENYTTINKFL SEVDAACVYA 

       370        380        390        400        410 
NASTRFTDGG EFGLGAEVGI STNKLHSRGP MGIEDLTTFK YKIYGQGQIR KG

A8EVN0 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