ID PROA2_BACLD Reviewed; 423 AA. AC Q65IS9; Q62U86; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 130. DE RecName: Full=Gamma-glutamyl phosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GPR 2 {ECO:0000255|HAMAP-Rule:MF_00412}; DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00412}; GN Name=proA2 {ECO:0000255|HAMAP-Rule:MF_00412}; GN OrderedLocusNames=BLi02148, BL01984; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5- CC phosphate into L-glutamate 5-semialdehyde and phosphate. The product CC spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. CC {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl CC 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, CC ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00412}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate CC 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_00412}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family. CC {ECO:0000255|HAMAP-Rule:MF_00412}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017333; AAU41035.1; -; Genomic_DNA. DR EMBL; CP000002; AAU23673.1; -; Genomic_DNA. DR RefSeq; WP_003182464.1; NC_006270.3. DR AlphaFoldDB; Q65IS9; -. DR SMR; Q65IS9; -. DR STRING; 279010.BL01984; -. DR GeneID; 92861261; -. DR KEGG; bld:BLi02148; -. DR KEGG; bli:BL01984; -. DR eggNOG; COG0014; Bacteria. DR HOGENOM; CLU_030231_0_0_9; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1. DR FunFam; 3.40.309.10:FF:000006; Gamma-glutamyl phosphate reductase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR HAMAP; MF_00412; ProA; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR012134; Glu-5-SA_DH. DR InterPro; IPR000965; GPR_dom. DR NCBIfam; NF001221; PRK00197.1; 1. DR NCBIfam; TIGR00407; proA; 1. DR PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1. DR PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS01223; PROA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase; KW Proline biosynthesis; Reference proteome. FT CHAIN 1..423 FT /note="Gamma-glutamyl phosphate reductase 2" FT /id="PRO_0000189694" SQ SEQUENCE 423 AA; 45601 MW; 38BBCA4EA7002357 CRC64; MTATSESISA QIEEKAIKAK TAAKSLRLAT EKEKNEALAA LADHLKQNMS YILTENAKDI EAGRKKGYDA AYIDRLSLNE DRVLDFADGL LEVAELDDPV GETLSSWTLD NGLKAEKVSV PLGVIGMIYE ARPNVTVDAT GLALKSGNAI VLKGGSSAIH SNTAIVSVMH QALDSTNIPR DAVQFIESTD RSATKQLFKM KEHIDVLIPR GGGALIQEVV ENATVPVLET GVGNCHIYID READPEKAID VMINAKTDRP AVCNALETLI VHEKWLEENS AALINALNEH GIQVHGDEKA VQMIPGARPA GEADWQNEYL SLDLAVKVAG SLEEACDHIE TYGTKHSEAI ITENPETAKA FLNTVDAAAL YHNASTRFTD GGALGFGAEI GISTQKLHAR GPMGLKELTT CKYIMRGDGH IRR //