ID   PROA_CUPTR              Reviewed;         426 AA.
AC   B3R6R0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RALTA_A2612;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ70543.1; -; Genomic_DNA.
DR   RefSeq; WP_012353839.1; NC_010528.1.
DR   AlphaFoldDB; B3R6R0; -.
DR   SMR; B3R6R0; -.
DR   STRING; 977880.RALTA_A2612; -.
DR   EnsemblBacteria; CAQ70543; CAQ70543; RALTA_A2612.
DR   GeneID; 29762489; -.
DR   KEGG; cti:RALTA_A2612; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_4; -.
DR   OMA; PGVCNAM; -.
DR   OrthoDB; 223669at2; -.
DR   BioCyc; CTAI977880:RALTA_RS12705-MON; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001692; Chromosome 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-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; 2.
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..426
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_1000193591"
SQ   SEQUENCE   426 AA;  45685 MW;  A8332162EF0D3247 CRC64;
     MTEFDLNQYM DRVGRQARAA SRAIARASTA DKNRALLTIA AAIRRDADQL KAVNARDVER
     ARANGQDAAF VDRLTLSDKA IATMAAGLEQ IAALPDPIGE ISNMKFRPTG IQVGQMRVPL
     GVIGIIYESR PNVTIDAAAL CLKSGNATIL RGGSEAIESN TALAALVAEG LSAAGLPPEA
     VQVIETTDRA AVGRLITMTE FVDVIVPRGG KSLIARLMEE ARVPMIKHLD GICHVYIDAE
     ADLDKAVRVC DNAKTQRYAP CNTMETLLVS QDIAAAALPP LCRIYQQKGV ELRVCPATRA
     TLEAAGFSGL VDASEEDWRL EYLAPILAIK TVVGLDQAIS HINEYGSHHT DSIITENYSA
     GMRFIREVDS ASVMINASTR FADGFEYGLG AEIGISNDKL HARGPVGLEG LTSLKYVVFG
     HGEVRT