[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Gross R., Linke B.; "Complete genome sequence of Bordetella petrii strain DSM 12804."; Submitted (DEC-2007) 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 (By similarity).
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

AM902716; CAP43669.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001631937.1; -.

3D structure databases

ModBase

A9HWX2.

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

5817350; -.

GenomeReviews

AM902716_GR; Bpet3327.

KEGG

bpt:Bpet3327; -.

CMR

A9HWX2; Bpet3327.

Other

ProtoNet

A9HWX2.

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`	`1 421`	`421`		`Gamma-glutamyl phosphate reductase.`	`PRO_0000340874`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 44216 Da [This is the MW of the unprocessed precursor]

CRC64: 21DF165E5DC69B75 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPATDIDTAM LALGENARRA SRAMMRATGA AKNHALQAMA EALRDNRAEL QAANAQDIDA 

        70         80         90        100        110        120 
ARAGGLEPAL LDRLTLSDKA IDRMAEGLLQ VAALPDPIGS TTASALRPNG MRVAQMRVPL 

       130        140        150        160        170        180 
GVIGIIYESR PNVTIDAAAL CLKSGNATIL RGGSEALHSN VALGRIVQAG LQAAALPAEA 

       190        200        210        220        230        240 
VQVVGTTDRA AVGKLITMTE HIDVIVPRGG KGLIARLASE ARVPLIKHLD GNCHVYIDAA 

       250        260        270        280        290        300 
ADPQKAHTIA FNAKTYRYGI CGAMETLLVD AGVAVSILPR LAAAFSAHGV ELRGCPRTLE 

       310        320        330        340        350        360 
IVPSATPATD DDWATEYLAP ILAVRIVDSL DQAIEHIARW GSGHTDAIVT EDLSAAQRFQ 

       370        380        390        400        410        420 
REVDSSSVYV NLPTCFADGF EYGLGAEIGI STNRLHARGP VGLEGLTTLK WVLNGDGQTR 


G

A9HWX2 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