ID PROA_GEOKA Reviewed; 414 AA. AC Q5KYA2; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GPR {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 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=GK2049; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of thermophilic RT Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(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 + NADP(+) + phosphate = H(+) + L- CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58066, 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; BA000043; BAD76334.1; -; Genomic_DNA. DR RefSeq; WP_011231535.1; NC_006510.1. DR AlphaFoldDB; Q5KYA2; -. DR SMR; Q5KYA2; -. DR STRING; 235909.GK2049; -. DR KEGG; gka:GK2049; -. DR eggNOG; COG0014; Bacteria. DR HOGENOM; CLU_030231_0_0_9; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000001172; 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-UniPathway. DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 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; 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..414 FT /note="Gamma-glutamyl phosphate reductase" FT /id="PRO_0000189728" SQ SEQUENCE 414 AA; 45650 MW; D57558B51B02E565 CRC64; MSELLEKAER LKTASQTLAM LSAEEKNEAL EQIAQTLDRE RAFILQENEK DMAQGREQGL SPALLDRLQL TNERLDQIID GVRQVASLPD PVGEIIAEWT RPNGLRIQTV RVPLGVIGMV YEARPNVTVD AASLCLKTGN AVLLRGSTSA LHSNKALVAV MKEALRTTAI PETAIELLED TSRETAQRMF RLNNYLDVLI PRGGAGLIRS VVENATVPVL ETGVGNCHIF VDESAERQMA IEIVLNAKLQ RPSVCNAVET VLIHERWPYA ADLLETLHAR GVELRGDQRL ASAYPFISEA TEDDWYTEYL APILAVKLVA DVDEAIGHIR RYGTKHSEAI ITENEVNVRR FFQAVDAAVL YHNASTRFTD GEQFGYGAEI GISTQKLHAR GPMGLVAITT TKSLVYGTGQ IRTV //