ID PROA_BURCH Reviewed; 423 AA. AC A0K4I3; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 2. DT 16-JUN-2009, entry version 22. DE RecName: Full=Gamma-glutamyl phosphate reductase; DE Short=GPR; DE EC=1.2.1.41; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase; DE Short=GSA dehydrogenase; GN Name=proA; OrderedLocusNames=Bcen2424_0657; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADPH dependent reduction of L-gamma- CC glutamyl 5-phosphate into L-glutamate 5-semialdehyde and CC phosphate. The product spontaneously undergoes cyclization to form CC 1-pyrroline-5-carboxylate (By similarity). CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000458; ABK07410.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_834303.1; -. DR GeneID; 4450758; -. DR GenomeReviews; CP000458_GR; Bcen2424_0657. DR KEGG; bch:Bcen2424_0657; -. DR HOGENOM; A0K4I3; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00412; -; 1. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR000965; Gglut_pp_reduct. DR InterPro; IPR012134; Glu-5-SA_DH. DR Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11063:SF1; GSA_DH; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS01223; PROA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Proline biosynthesis. FT CHAIN 1 423 Gamma-glutamyl phosphate reductase. FT /FTId=PRO_0000340875. SQ SEQUENCE 423 AA; 45185 MW; 604ADE6D375D161A CRC64; MDIDQYMTDL GRRARHASRA MARASTAAKN AALDAVARAI ERDAQALKDA NARDVARARE KGLDAAFIDR LTLSDKALNT MVEGLRQVAS LADPIGEIGN LKFRPSGIQV GQMRVPLGVI GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNAAL AKLIGEGLEA AGLPQDAVQV VATADRAAVG KLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRADL AKALTVCDNA KTHRYGTCNT METLLVASGI AAKLLPPLGK LYRDKQVELR VDAAARAVLA DAGVGPLVDV TEEDWHTEYL APVLAIKVVD GLDAAIEHIN HYGSHHTDAI VTEDHDRAMR FLREVDSASV MVNASTRFAD GFEFGLGAEI GISNDKLHAR GPVGLEGLTS LKYVVLGHGE GRQ //