ID   PROA_THET8              Reviewed;         413 AA.
AC   Q5SH02;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=TTHA1928;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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 + 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; AP008226; BAD71751.1; -; Genomic_DNA.
DR   RefSeq; WP_011229021.1; NC_006461.1.
DR   RefSeq; YP_145194.1; NC_006461.1.
DR   AlphaFoldDB; Q5SH02; -.
DR   SMR; Q5SH02; -.
DR   STRING; 300852.55773310; -.
DR   EnsemblBacteria; BAD71751; BAD71751; BAD71751.
DR   GeneID; 3169314; -.
DR   KEGG; ttj:TTHA1928; -.
DR   PATRIC; fig|300852.9.peg.1899; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_0; -.
DR   OMA; PGVCNAM; -.
DR   PhylomeDB; Q5SH02; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000000532; 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..413
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189804"
SQ   SEQUENCE   413 AA;  45854 MW;  944FDA42C7866ECA CRC64;
     MTATSLWELA ERARKRLSEI AKGNRDRALL AMADLLEARW EEVLRANRED LEEAERTGLP
     KAKLDRLALK EKDLKTLTEG LRQIARLPDP LGRIEGLAKR PNGLRVGRMR VPLGLIGFIY
     EARPGATVEA VSVALKAGNA MLLRGGKEAF RSNRALVALW HEALGEAGLP EEAVTLVPTT
     DREAVLEMCR LELLDLLIPR GGEELIRLVQ REARVPVLAH AKGVNHLYVD KKADLSMALR
     LALNGKTQRP AVCNALETVL VHEKVAEAFL PRLEKAMREK GVELRACPRA LPLLKEAVPA
     REDEWDREYL DLVLRVKVVS GLEEALAHIA RYGSRHTEAI CTEDPKAAWR FLEEVDASLV
     LWNASTRFND GFELGLGAEI GISTSKLHAY GPMGPMELTT LKWVALGEGQ ERT