ID   PROA_BRASO              Reviewed;         429 AA.
AC   A4YKF1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=BRADO0430;
OS   Bradyrhizobium sp. (strain ORS278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=114615;
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; CU234118; CAL74377.1; -; Genomic_DNA.
DR   RefSeq; YP_001202623.1; -.
DR   GeneID; 5116228; -.
DR   GenomeReviews; CU234118_GR; BRADO0430.
DR   KEGG; bra:BRADO0430; -.
DR   OMA; A4YKF1; 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_1000049938.
SQ   SEQUENCE   429 AA;  45095 MW;  A500F9D664824371 CRC64;
     MTAPLKAIDG SADLPQLMND LAKRARAAAR VLALAPAEQK NRALEAMERR IRARADVIIA
     ANAEDVAEAK AVGVTPSFVD RLTLTPARVA AMADGIAVVR GVADPVGVVT ESWQRPNGMT
     IERVRVPLGV IGVIFESRPN VAADAGVLCL KSGNAVILRG GSDSFRSCRA IHECLVEGLR
     EAGLPDTAIT LVPTRDRAAV GLLLSGLNGG VDVIVPRGGK SLVARVEAEA RVPVFAHLEG
     VNHVYVDGAA DLDMAKSIVL NAKMRRTGVC GAAETLLIDR ASQDKIKPLV DMLIGAGCEV
     RGDEAVRAAD ARVTPANNED WDTEYLDAII AAKVVDGVDG AIAHIHAHGS HHTDAIVTQD
     NKVADKFLNE VDSAIVLHNA STQFADGGEF GFGAEIGIAT GKFHARGPVG VEQLTSFKYR
     IHGTGQTRP
//