PROA_SALTY
ID PROA_SALTY Reviewed; 416 AA.
AC P40861;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 143.
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=STM0322;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 394-416.
RC STRAIN=LT2;
RX PubMed=2984205; DOI=10.1016/s0021-9258(18)89288-2;
RA Leong J.M., Nunes-Dueby S., Lesser C.F., Youderian P., Susskind M.M.,
RA Landy A.;
RT "The phi 80 and P22 attachment sites. Primary structure and interaction
RT with Escherichia coli integration host factor.";
RL J. Biol. Chem. 260:4468-4477(1985).
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; AE006468; AAL19278.1; -; Genomic_DNA.
DR EMBL; M10894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_459319.1; NC_003197.2.
DR RefSeq; WP_000893231.1; NC_003197.2.
DR AlphaFoldDB; P40861; -.
DR SMR; P40861; -.
DR STRING; 99287.STM0322; -.
DR PaxDb; P40861; -.
DR EnsemblBacteria; AAL19278; AAL19278; STM0322.
DR GeneID; 1251841; -.
DR KEGG; stm:STM0322; -.
DR PATRIC; fig|99287.12.peg.343; -.
DR HOGENOM; CLU_030231_0_0_6; -.
DR OMA; PGVCNAM; -.
DR PhylomeDB; P40861; -.
DR BioCyc; SENT99287:STM0322-MON; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000001014; 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..416
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000189778"
SQ SEQUENCE 416 AA; 44665 MW; 490D0B1F039A0C98 CRC64;
MLEQMGIAAK AASYKLALLS SGEKNRVLEK IADELEAQME SILSANVQDV EQARANGLSE
AMLDRLALTP ARLKAIADDV RQVCNLADPV GQVIDGGLLD SGLRLERRRV PLGVVGVIYE
ARPNVTVDVA SLCLKTGNAV ILRGGKETYR TNAATVRVIQ KALKACGLPE AAVQAIDNPD
RSLVNEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIFVD SSADIAPALK
IIVNAKTQRP STCNTVETLL VHQDIAERFL PALSKQMAES GVTLHGDETV MQVLHGPAKL
VPLKPEELDN EFLSLDLNVV VVENMDGAIA HIREHGTQHS DAILTCDMHN AARFVNEVDS
AAVYVNASTR FTDGGQFGLG AEVAVSTQKL HARGPMGLEA LTTYKWIGFG DGTIRA
