PROA_THEYD
ID PROA_THEYD Reviewed; 418 AA.
AC B5YK66;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=THEYE_A0790;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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; CP001147; ACI21133.1; -; Genomic_DNA.
DR RefSeq; WP_012545857.1; NC_011296.1.
DR RefSeq; YP_002248631.1; NC_011296.1.
DR AlphaFoldDB; B5YK66; -.
DR SMR; B5YK66; -.
DR STRING; 289376.THEYE_A0790; -.
DR EnsemblBacteria; ACI21133; ACI21133; THEYE_A0790.
DR KEGG; tye:THEYE_A0790; -.
DR PATRIC; fig|289376.4.peg.780; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_0; -.
DR InParanoid; B5YK66; -.
DR OMA; PGVCNAM; -.
DR OrthoDB; 223669at2; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
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; 1.
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; Reference proteome.
FT CHAIN 1..418
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_1000193670"
SQ SEQUENCE 418 AA; 46594 MW; 98A03FEBFC1E9C09 CRC64;
MEIKQLVLNK AKEAKESSRF IAKASTDLKN KIIVRMADYL KQNKDELIKA NRIDVENAQK
KGISKALIDR LTLTEKRIDE MIKGLQEVVA LPDPVGEITK MWLRPNGMQV GKMRVPIGVI
GVIYEARPNV TVDVTGLCLK AGNSVVLRGG SEAINSNIAL VKILKEALKD EGMHEGVVTY
IDISQREAVL EMIKLEGIID LIIPRGGEGL IRTVTENSRI PVLKHYKGVC HVFVDRDADL
AMAEEICFNA KVQRPATCNA METMLVDENI AKKFLPNMLK KFEDAGVELK GCLKTKKIYP
KVKDVKEEDF YQEYLDLVLN VKVVKNIDEA IEHITKYGSA HSDSIVTKDY NKAMKFLKEV
DSSAVFVNAS TRLNDGYQFG LGAEIGISTD KIHARGPMGL EELTCTKFIV FGNGQIRQ
