ID A0A359K326_ALTSX Unreviewed; 415 AA. AC A0A359K326; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 25-MAY-2022, entry version 11. DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412}; DE Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412}; DE EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412}; GN Name=proA {ECO:0000256|HAMAP-Rule:MF_00412}; GN ORFNames=DEH24_07125 {ECO:0000313|EMBL:HBY39168.1}; OS Alteromonas sp. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas. OX NCBI_TaxID=232 {ECO:0000313|EMBL:HBY39168.1, ECO:0000313|Proteomes:UP000262181}; RN [1] {ECO:0000313|EMBL:HBY39168.1, ECO:0000313|Proteomes:UP000262181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9522 {ECO:0000313|EMBL:HBY39168.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:0000256|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:0000256|ARBA:ARBA00000979, ECO:0000256|HAMAP- CC Rule:MF_00412}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate CC 5-semialdehyde from L-glutamate: step 2/2. CC {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}. CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family. CC {ECO:0000256|HAMAP-Rule:MF_00412}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HBY39168.1}. 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; DOSX01000190; HBY39168.1; -; Genomic_DNA. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000262181; Unassembled WGS sequence. 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 Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS01223; PROA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00412}; KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP- KW Rule:MF_00412}. FT DOMAIN 11..279 FT /note="Aldedh" FT /evidence="ECO:0000259|Pfam:PF00171" SQ SEQUENCE 415 AA; 44401 MW; BB6BB3ADAF285A53 CRC64; MSLITNIAND TARAAKVLAV LDEQTKNNVL ADMAAAIRGA AEHIIEVNAA EVAAGKAAGL DEAMEDRLTL TPARIEDMAQ GIETIISLDD PVGKERHITD RPNGLKIQKM RVPLGVVCMI YEARPNVTAD AGALCFKSGN GVILRGGKEA LNTSLAIAGL LQEVLRKHQL PEALISVIPD PDRGLMQELM EQTETIDVII PRGGEGLIRY VTDNSKVPVI QHFKGVCHLY VDKDADLTMA MDLLVNGKTQ RTGVCNALEG LVVHQAVAGD FLPQVSAMCQ EKGVTVHVNQ AGAAYFSEAD VIADDAFGEE YLGPEIAIRV VDDFNQALAH IDQFGSHHTE VICTQNAETA RLFQRVVDAS AVMVNASSRF NDGSQLGLGA EIGIATTKLH AYGPMGLESL TTEKYVVSGT GQVRE //