ID   PROA_STRMU              Reviewed;         416 AA.
AC   Q8DVM9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   28-JAN-2026, entry version 137.
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=SMU_450;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58200.1; -; Genomic_DNA.
DR   RefSeq; WP_002262086.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVM9; -.
DR   SMR; Q8DVM9; -.
DR   STRING; 210007.SMU_450; -.
DR   KEGG; smu:SMU_450; -.
DR   PATRIC; fig|210007.7.peg.396; -.
DR   eggNOG; COG0014; Bacteria.
DR   HOGENOM; CLU_030231_0_0_9; -.
DR   OrthoDB; 9809970at2; -.
DR   PhylomeDB; Q8DVM9; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000002512; 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-UniRule.
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   NCBIfam; NF001221; PRK00197.1; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 2.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; ALDH-like; 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..416
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189787"
SQ   SEQUENCE   416 AA;  45219 MW;  40EB07C1D5D68A79 CRC64;
     MAIIDNLGQN AKKASFLLAQ LGTEAKNTAL LKVAEALLAE LPYILEENAK DVALAQEHGI
     SAIMVDRLRL DEKRLQDIAS GVRDVAALGD PIGQVVRGYT NMVGLKIIQK RVPLGVIAMI
     FESRPNVSVD AFSLAFKTGN AIILRGGRDA ICSNTALVNV IRRTLASFGL DENAVQLVED
     TSHEVAKELM AAVDYVDVLI PRGGARLIQT VKKEAKVPVI ETGVGNVHIY VDEFADLDMA
     SKIVVNAKTQ RPSVCNAAEG LLVHEKVASD FLPKLEAAIN QIHPVEFRAD DRAQKILKNA
     QPASQEDYAT EFLDYIISVK IVNSLGEAID WINTYTSHHS ESIITRDIQA AERFQDEVDA
     AAVYVNASTR FTDGFVFGLG AEIGISTQKL HARGPMGLEA LTSTKFYING KGQIRE
//