ID PROA_SYNE7 Reviewed; 431 AA.
AC Q31KX4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=Synpcc7942_2265;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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: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; CP000100; ABB58295.1; -; Genomic_DNA.
DR RefSeq; WP_011244143.1; NZ_CP130602.1.
DR AlphaFoldDB; Q31KX4; -.
DR SMR; Q31KX4; -.
DR STRING; 1140.Synpcc7942_2265; -.
DR PaxDb; 1140-Synpcc7942_2265; -.
DR GeneID; 76400995; -.
DR KEGG; syf:Synpcc7942_2265; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_1_3; -.
DR OrthoDB; 9809970at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2265-MONOMER; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000889800; 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; 1.
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..431
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000252602"
SQ SEQUENCE 431 AA; 45745 MW; 90A19627E71E1250 CRC64;
MATLSVDLEV QAQATRAAAR QLAQWSGADR QRLLSAIATT LEQEAPRILA ANQADCEAAT
TEGIAPALYA RLKLDADKLA AAIAGVRDLA QLPDPLGQIQ IDRELDEGLI LQRLTCPVGV
LGVIFEARPD AVIQIASLAI KSGNGAILKG GREAICSCQA IVAAIAQALA EQQAPVEAIR
LLTSREETLA LLKLDRYVDL IIPRGSNSFV RFVQDNTHIP VLGHADGICH LYVDQAAAIE
KTVTITVDAK TQYPAACNAI ETLLIHEAIA PQFLPVVAAA LHEKGVSLRG DAAAQTIVPM
EAATEEDWRT EYSDLVLAVR LVPSLDAAIA HINEYGSGHT DAIATEDAAA AAQFFSQVDS
AGVYHNCSTR FADGFRYGFG AEVGISTQKL PPRGPVGLEG LVTYKYVLSG DGQIAATYSG
AQAKPFLHRD R
//
