ID   PROA_BRASB              Reviewed;         429 AA.
AC   A5E961;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=BBta_0419;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA   Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L.,
RA   Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P.,
RA   Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A.,
RA   Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic
RT   bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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.
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; CP000494; ABQ32705.1; -; Genomic_DNA.
DR   RefSeq; YP_001236611.1; -.
DR   GeneID; 5155258; -.
DR   GenomeReviews; CP000494_GR; BBta_0419.
DR   KEGG; bbt:BBta_0419; -.
DR   OMA; A5E961; APIISIK.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH 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; IPR016162; Ald_DH_N.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11063:SF1; GSA_DH; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   TIGRFAMs; TIGR00407; proA; 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    429       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_1000049937.
SQ   SEQUENCE   429 AA;  44873 MW;  B44F092B9EA27EE3 CRC64;
     MTAPLKAIDG SADLPALMND LASRARAAAR VLALAPAAQK NRALEAMERL IRARVDTIIA
     ANAEDVVEAK AAGITSSFLD RLTLTPARVA AMADGIAAVR EVADPIGIVT ESWQRPNGMT
     IERVRVPLGV IGVIFESRPN VAADAGVLCL KSGNAVILRG GSDSFRSCRA IHECLVEGLR
     EAGLPDAAIT LVPTRDRAAV GLLLSGLNGG VDVIVPRGGK NLVARVEAEA RVPVFAHLEG
     VNHVYVDGAA DLEMAKSIVL NAKMRRTGVC GAAETLLIDR ASQDKIKPLV DTLINAGCEV
     RGDDAVRAAD ARVKPASNED WDTEYLDAVI AAKVVDGVEG AIAHIQAHGS HHTDAIVTAD
     VAAADKFLNE VDSAIVLHNA STQFADGGEF GFGAEIGIAT GKFHARGPVG VEQLTSFKYR
     IHGTGQTRP
//