ID   PROA_CORML              Reviewed;         432 AA.
AC   P0C1E1; P45638;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
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   Corynebacterium melassecola.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=41643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17965 / AS B-4821;
RX   PubMed=8522535; DOI=10.1128/jb.177.24.7255-7260.1995;
RA   Serebrijski I., Wojcik F., Reyes O., Leblon G.;
RT   "Multicopy suppression by asd gene and osmotic stress-dependent
RT   complementation by heterologous proA in proA mutants.";
RL   J. Bacteriol. 177:7255-7260(1995).
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; X82929; CAA58103.1; -; Genomic_DNA.
DR   PIR; S49980; S49980.
DR   AlphaFoldDB; P0C1E1; -.
DR   SMR; P0C1E1; -.
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..432
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000236036"
SQ   SEQUENCE   432 AA;  45643 MW;  5630EA65B29B0682 CRC64;
     MSSTTLTDDQ IRDNERTEVL AKATAAKNIV PDIAVLGTGP KNAILRAAAD ELVARSAEII
     EANASDIEAG RANGMEESMI DRLALDESRI EGIAGGLRQV AGLTDPVGEV LRGHVMENGI
     QMKQVRVPLG VMGMVYEARP NVTVDAFALA LKSGNVAFVR GSSTAVHSNT KLVEILQDVL
     ERFELPRETV QLLPCQTRGS VQDLITARGL VDVVIPRGGA GLINAVVTGA TVPTIETGTG
     NCHFYIDAEA KLGQAIAMVI NGKTRRCSVC NATETALLDA ALSDSDKLAV VQALQEAGVT
     IHGRVAELEA FGATDVVEAT ETDWDSEYLS FDIAVAVVDG VDGALAHIAK YSTKHTEAIA
     TQNIETAQRF ADRVDAAAVM INASTAYTDG EQYGMGAEIG ISTQKLHARG PMALPELTST
     KWILQGTGQI RP