PROA_PARD8
ID PROA_PARD8 Reviewed; 415 AA.
AC A6LE74;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BDI_2257;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43988.1; -; Genomic_DNA.
DR RefSeq; WP_011966792.1; NC_009615.1.
DR AlphaFoldDB; A6LE74; -.
DR SMR; A6LE74; -.
DR STRING; 435591.BDI_2257; -.
DR EnsemblBacteria; ABR43988; ABR43988; BDI_2257.
DR KEGG; pdi:BDI_2257; -.
DR PATRIC; fig|435591.13.peg.2242; -.
DR eggNOG; COG0014; Bacteria.
DR HOGENOM; CLU_030231_0_0_10; -.
DR OMA; PGVCNAM; -.
DR OrthoDB; 223669at2; -.
DR BioCyc; PDIS435591:G1G5A-2320-MON; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000566; 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 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; IPR012134; Glu-5-SA_DH.
DR InterPro; IPR000965; GPR_dom.
DR PIRSF; PIRSF000151; GPR; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..415
FT /note="Gamma-glutamyl phosphate reductase"
FT /id="PRO_0000340900"
SQ SEQUENCE 415 AA; 45817 MW; 99DF1DED71ECCC1C CRC64;
MNVKDMLRQA SDAAKQLITL SDQTIIGILK ETAQVLRTHT EEVLAANRQD LERMDPANPK
YDRLKLTEER LQGIAADMEN VSTLPSPLNK VLSETIRPNG MVIRKVTVPF GVIGVIYEAR
PNVTFDVFSL CFRSGNACVL KGGSDADFSN RALVRIIHSV LERQGINPAV CTLLPPDREA
TAELLGAVGL VDLIIPRGSS SLIHFVREHA KVPVIETGAG ICHTYFDRSG DKGKGREIVN
NAKTRRVSVC NALDCLIIHR ERLSDLPYIC EKLPDSNVII YADEPAYAAL SEHYPETLLQ
QANENSFGTE FLDYKMSIRT VSSLDEVLSH IARYSSKHSE SIISEDPETI RRFQQLVDAA
CVYANVSTAF TDGAQFGFGA EIGISTQKLH ARGPMALPEL TTYKYIIEGD GQTRI