ID   PROA_CHLSY              Reviewed;         422 AA.
AC   B9LE47;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   04-NOV-2026, entry version 78.
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};
GN   OrderedLocusNames=Chy400_1753;
OS   Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Chloroflexineae; Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=480224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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 + phosphate + NADP(+) = L-glutamyl
CC         5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066,
CC         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; CP001364; ACM53163.1; -; Genomic_DNA.
DR   SMR; B9LE47; -.
DR   KEGG; chl:Chy400_1753; -.
DR   HOGENOM; CLU_030231_0_0_0; -.
DR   OMA; AACIYVN; -.
DR   OrthoDB; 9809970at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   FunFam; 3.40.309.10:FF:000006; Gamma-glutamyl phosphate reductase; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   NCBIfam; NF001221; PRK00197.1; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   PROSITE; PS01223; PROA; 1.
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-UniRule.
DR   AlphaFoldDB; B9LE47; -.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis.
FT   CHAIN           1..422
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_1000193586"
SQ   SEQUENCE   422 AA;  44515 MW;  68BC84715CCE3378 CRC64;
     MVDLEAIGRR AKTAARALAK LSTEQKNAAL CAIADGLLAR QDKILAANAA DVADAEKGGT
     PPAIVDRMLL TPARLAAIAG DCRQVASLPD PVGEIFDRRE LPSGLRLYKR RVPIGVIGAI
     YEARPNVTVD IASLCLKAGN AVILRGGSDI ARSVAATTEV IALALEQAGL PAFAVQSIID
     PDRELVRQLL RLDRYVDMII PRGGAGLHRF CVENATVPVI VGGMGVSHIY VEPSADFARA
     VPVIVNAKVQ RPGACNALDT LLVHRAAAST FLPLVAAALA QHGVELRCDL EALAILADAP
     GHEAWNLKPA SPTDFGCEFL ALIVAIKIVG SIDEALDHIA LYGGHSEAIL TGDPISAERF
     TREVDATAVF VNASTRFNDG GQFGLGAEVA ISTNRLHARG PMGLQELTTY TWIGEGDYLV
     RA
//