ID   PROA_STRTR              Reviewed;         416 AA.
AC   P96489;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
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};
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19258 / DSM 20617 / LMG 6896 / NCDO 573 / NCIMB 8510;
RX   PubMed=8969524; DOI=10.1099/13500872-142-11-3275;
RA   Limauro D., Falciatore A., Basso A.L., Forlani G., de Felice M.;
RT   "Proline biosynthesis in Streptococcus thermophilus: characterization of
RT   the proBA operon and its products.";
RL   Microbiology 142:3275-3282(1996).
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; X92418; CAA63148.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96489; -.
DR   SMR; P96489; -.
DR   STRING; 322159.STER_1675; -.
DR   eggNOG; COG0014; Bacteria.
DR   UniPathway; UPA00098; UER00360.
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..416
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189794"
SQ   SEQUENCE   416 AA;  45390 MW;  518F4538B0981FFB CRC64;
     MTYVDTLGQQ AKVASRQIAK LSTAAKNDLL NQVAKALVAE SDYIFTENAK DMANASENGI
     SKIMQDRLLL TEDRIAGIAE GVRQVADLQD PIGQVVRGYT NLDGLKIVQK RVPMGVIAMI
     FESRPNVSID AFSLAFKTNN AIILRGGRDA INSNKALVTV ARKALKNAGI TADAVQFVED
     TSHEVAEELM VATKYVDLLI PRGGARLIQT VKEKAKVPVI ETGVGNCHIY VDKYANLDMA
     TQIVINAKTQ RPSVCNAAES LVVHADIVEE FLPNLEKAIS KIQSVEFRAD ERALKLMEKA
     VPASPEDFAT EFLDYIMSVK VVDSLDEAIN WINTYTTSHS EAIVTQDISR AEQFQDDVDA
     AAVYVNASTR FTDGFVFGLG AEIGISTQKM HARGPMGLEA LTSTKFYING QGQIRE