ID PROA_STRA5 Reviewed; 417 AA.
AC Q8E1R9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 18-JUN-2025, entry version 126.
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=SAG0284;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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; AE009948; AAM99191.1; -; Genomic_DNA.
DR RefSeq; NP_687319.1; NC_004116.1.
DR RefSeq; WP_000221014.1; NC_004116.1.
DR AlphaFoldDB; Q8E1R9; -.
DR SMR; Q8E1R9; -.
DR STRING; 208435.SAG0284; -.
DR KEGG; sag:SAG0284; -.
DR PATRIC; fig|208435.3.peg.282; -.
DR HOGENOM; CLU_030231_0_0_9; -.
DR OrthoDB; 9809970at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000821; 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..417
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189784"
SQ SEQUENCE 417 AA; 45570 MW; 8210BFC21D1CE665 CRC64;
MTYIEILGQN AKKASQSVAR LSTASKNEIL RDLARNIVAD TETILTENAR DVVKAKDNGI
SEIMVDRLRL NKDRIQAIAN GIYQVADLAD PIGQVVSGYT NLDGLKILKK RVPLGVIAMI
FESRPNVSVD AFSLAFKTGN AIILRGGKDA IFSNTALVNC MRQTLQDTGH NPDIVQLVED
TSHVVAEELM QATDYVDVLI PRGGAKLIQT VKEKSKIPVI ETGVGNVHIY IDEFADLDMA
AKIVINAKTQ RPSVCNAAEG LVVHQAIAKG FLSQLEKMLK ESNQSVEFRA DEEALQLLEN
AVAASESDYA TEFLDYIMSV KVVDSFEQAI SWINKYSSHH SEAIITNNIS RAEIFQDMVD
AAAVYVNAST RFTDGFVFGL GAEIGISTQK LHARGPMGLE ALTSTKYYIN GTGQVRE
//
