NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) 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

CP000151; ABB07344.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_367988.2; -.

3D structure databases

ModBase

Q39JM2.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A3743-MON; -.

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:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
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

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

3748927; -.

GenomeReviews

CP000151_GR; Bcep18194_A3743.

KEGG

bur:Bcep18194_A3743; -.

NMPDR

fig|269483.3.peg.5384; -.

Phylogenomic databases

HOGENOM

Q39JM2; -.

Genome annotation databases

CMR

Q39JM2; Bcep18194_A3743.

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`	`1 423`	`423`		`Gamma-glutamyl phosphate reductase.`	`PRO_0000229995`

Sequence information

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

Molecular weight: 45279 Da [This is the MW of the unprocessed precursor]

CRC64: 1ED5D01D489288BD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDIDQYMTDL GRRARHASRA MARASTAAKN AALDAVARAI ERDAQVLKDA NARDVARARE 

        70         80         90        100        110        120 
KGLDAAFVDR LTLSDKALNT MVEGLRQVAS LADPIGEISN LKYRPSGIQV GQMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLEA AGLPQDAVQV 

       190        200        210        220        230        240 
VATADRAAVG KLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRADL 

       250        260        270        280        290        300 
AKALTVCDNA KTHRYGTCNT METLLVSSGV AAKLLPPLGK LYRDKQVELR VDAAARTVLA 

       310        320        330        340        350        360 
DAGVGPLVDA TEEDWHTEYL APVLAIKVVD GLDAAIEHIN HYGSHHTDAI VTEDHDRAMR 

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


GRQ

Q39JM2 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