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   25-MAY-2022, entry version 103.
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; Firmicutes; 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}.
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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   EnsemblBacteria; BAD76334; BAD76334; GK2049.
DR   KEGG; gka:GK2049; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_9; -.
DR   OMA; PGVCNAM; -.
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   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..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