ID   PROA_DESHY              Reviewed;         417 AA.
AC   Q24XR6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=DSY1387;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE83176.1; -; Genomic_DNA.
DR   RefSeq; WP_011459658.1; NC_007907.1.
DR   AlphaFoldDB; Q24XR6; -.
DR   SMR; Q24XR6; -.
DR   STRING; 138119.DSY1387; -.
DR   PRIDE; Q24XR6; -.
DR   EnsemblBacteria; BAE83176; BAE83176; DSY1387.
DR   KEGG; dsy:DSY1387; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_9; -.
DR   OMA; PGVCNAM; -.
DR   OrthoDB; 223669at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001946; 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   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; Reference proteome.
FT   CHAIN           1..417
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000252570"
SQ   SEQUENCE   417 AA;  45021 MW;  104F97D1A0D75BCE CRC64;
     MDFAPELITI GQKAKDAARK LAYAGTAAKN KALLAMAEAL LNHEQKILEA NRKDVEAAIQ
     KGTKKSLVNR LALTSEGIRQ MSDALKEVVN LGDPVGEGEF WTRPNGLRIQ RTRVPLGVVA
     MIYEARPNVT VDAAALCLKS GNAVILRGGS EAIESNKILS KVIAGAAESQ GMPTACIQLL
     ENTNRQWVQQ LMKMNGYVDV IIPRGGAGLI ETVVKEATVP VIETGTGVCH AYVDGEADLA
     KGVSIVFNAK TQKPGVCNAL EAVLVNEAVA QEFLPLLGEK FRDYGVEIRG CEKTCAILPY
     AAKATEEDWG TEYLDLIISA KVVQGVDEAM DHIYQYGTKH SETIITENYT TAQRFLNEVD
     AAAVYVNAST RFTDGGRFGF GAEIGISTQK LHARGPMGLQ ALTTMKYMVY GEDHIVT