ID   PROA_CAUSK              Reviewed;         419 AA.
AC   B0T315;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-NOV-2008, entry version 8.
DE   RecName: Full=Gamma-glutamyl phosphate reductase;
DE            Short=GPR;
DE            EC=1.2.1.41;
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
DE            Short=GSA dehydrogenase;
GN   Name=proA; OrderedLocusNames=Caul_4717;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH dependent reduction of L-gamma-
CC       glutamyl 5-phosphate into L-glutamate 5-semialdehyde and
CC       phosphate. The product spontaneously undergoes cyclization to form
CC       1-pyrroline-5-carboxylate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family.
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DR   EMBL; CP000927; ABZ73837.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001686335.1; -.
DR   GeneID; 5902179; -.
DR   GenomeReviews; CP000927_GR; Caul_4717.
DR   KEGG; cak:Caul_4717; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00412; -; 1.
DR   InterPro; IPR016163; Ald_DHase_C.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DHase.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
FT   CHAIN         1    419       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000340876.
SQ   SEQUENCE   419 AA;  43111 MW;  D91003013D3509AB CRC64;
     MSLQATMTAM GQAARQGASA LRVATPAQRT AALHAMAAAI RADAPAILAA NAKDLEKAGA
     GGLTAPMVER LMLNPERLED VAAGVEAVAA IPDPLGVETA RWTRPNGLDI ARVRTPIGVI
     AMIFESRPNV TADAAALCVR SGNAVILRGG SECIHSNLAI HAAIAKGLKA AGISSDAVQI
     VRTPDRDAVG AILGGLNRTI DLIIPRGGKS LVARVQAEAR VAVLGHLEGL NHVFVHAAAD
     PRKAVEIVLN AKMRRVSVCG SAETLLVDRA AAERLLPPIA DALIKAGCEL RGDGPSRAIE
     PTMKPAVEAD WSTEYLAPVI SVAVVDGVEG AAAHIAAYGS GHTDAIVTED VAAAERFIAL
     VDSAIVLVNA STQFADGGEF GFGAEIGIAT DKLHARGPVG AEQLTTFKYV VRGTGQTRP
//