ID   PROA_SERMA              Reviewed;         417 AA.
AC   P17857;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 125.
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};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41;
RX   PubMed=1851803; DOI=10.1099/00221287-137-3-509;
RA   Omori K., Suzuki S., Imai Y., Komatsubara S.;
RT   "Analysis of the Serratia marcescens proBA operon and feedback control of
RT   proline biosynthesis.";
RL   J. Gen. Microbiol. 137:509-517(1991).
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}.
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DR   EMBL; D90351; BAA14365.1; -; Genomic_DNA.
DR   EMBL; X53086; CAA37255.1; -; Genomic_DNA.
DR   PIR; B49753; RDSEEM.
DR   RefSeq; WP_015376739.1; NZ_WVHW01000007.1.
DR   AlphaFoldDB; P17857; -.
DR   SMR; P17857; -.
DR   STRING; 273526.SMDB11_0225; -.
DR   GeneID; 64309772; -.
DR   UniPathway; UPA00098; UER00360.
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; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis.
FT   CHAIN           1..417
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189779"
SQ   SEQUENCE   417 AA;  44640 MW;  0E7264C4356F9D01 CRC64;
     MLEQMGKAAK QASWQLAVLS TAKKNQVLSV MADRLEANSE AILLANEQDM AQARATGMSE
     ALLDRLLLTP ARLAAIANDV RQVCRLNDPV GHVLDGNLLD SGLKLERRRV PLGVIGVIYE
     ARPNVTIDVA SLCLKTGNAV ILRGGKETHN TNQATVKVIQ QALEQCGLPA AAVQAIDSPD
     RALVNELLRL DRYVDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHTYVD ADVDFDKALT
     VIENAKIQRP SACNSLETLL VNRSIAAEFL PALSAKMAAA GVTLHAAENA LPLLQGGPAT
     VVPVNAEDYD DEWLSLDLNV LLVDDIDQAI DHIRTHGTNH SDAILTRSLS SAEHFVRAVD
     SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLD ALTTYKWIGY GDDLVRS