ID A0A3S9H9X9_9LACT Unreviewed; 422 AA.
AC A0A3S9H9X9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN Name=proA {ECO:0000256|HAMAP-Rule:MF_00412};
GN ORFNames=EJN90_05315 {ECO:0000313|EMBL:AZP04134.1};
OS Jeotgalibaca ciconiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=2496265 {ECO:0000313|EMBL:AZP04134.1, ECO:0000313|Proteomes:UP000273326};
RN [1] {ECO:0000313|Proteomes:UP000273326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H21T32 {ECO:0000313|Proteomes:UP000273326};
RA Bae J.-W., Lee S.-Y.;
RT "Complete genome sequencing of Jeotgalibaca sp. H21T32.";
RL Submitted (DEC-2018) 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:0000256|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:0000256|ARBA:ARBA00000979, ECO:0000256|HAMAP-
CC Rule:MF_00412};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_00412}.
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DR EMBL; CP034465; AZP04134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9H9X9; -.
DR KEGG; jeh:EJN90_05315; -.
DR OrthoDB; 9809970at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000273326; 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 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; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00412};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_00412}.
FT DOMAIN 8..294
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 309..405
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 422 AA; 45908 MW; 92CD776EEB7B0E22 CRC64;
MIGLLHQMGK QARKAANELR KTKTAKKNEA LLAMEQVLYK NEKQIIDANQ QDIQNAQANG
LPTPMIERLT LNSDRIKGMA DSIHQIAQLA DPVGYIEEMI TSEDGLKIGK QRVPLGVIGI
IYESRPNVTA DAAALCFKSG NAVILRGGKE ALHSNKAILA ALQEALVSVG LSEDTIQLIT
DPSRELAAEF MRMNEYLDCL IPRGGAGLIQ NVLKNATVPV IETGVGNCHL YVDEAADLKM
ATRILVNAKA DRPSVCNAIE NLVIHEAVSE EFLPVFADAL KEHHIEIRGD EKTQALVPEV
IAVEAEDYNT EFLDTVLAVK VVKDYGEAIS HIQEHSTGHS EVIVTDNYQT AQEFLEDIDA
AAVYVNASSR FTDGGCFGLG GEIGISTQKL HARGPMGLKE LTSYKYIIFG EGQIRGTTGA
EY
//
