ID   PROA_BRUSU              Reviewed;         421 AA.
AC   Q8FYM3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
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=BR1843;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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; AE014291; AAN30738.1; -; Genomic_DNA.
DR   RefSeq; NP_698823.1; -.
DR   HSSP; Q9WYC9; 1O20.
DR   GeneID; 1167536; -.
DR   GenomeReviews; AE014291_GR; BR1843.
DR   KEGG; bms:BR1843; -.
DR   NMPDR; fig|204722.1.peg.1780; -.
DR   TIGR; BR1843; -.
DR   HOGENOM; Q8FYM3; -.
DR   OMA; Q8FYM3; APIISIK.
DR   BioCyc; BSUI204722:BR_1843-MON; -.
DR   BRENDA; 1.2.1.41; 281610.
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; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
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    421       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189707.
SQ   SEQUENCE   421 AA;  44099 MW;  875A0863AC4F966D CRC64;
     MTKDIAQVMA EVGRKAKAAA APLSIATSEQ KNKALNAAAD AILEARADIL EANRLDLANA
     EKNGMAASFV DRLTLNEARI DAIAEDIRAI ATLPDPVGEV IAEWDRPNGL HIERVRTPLG
     VIGVIYESRP NVTADAGALC LKAGNAVILR GGSDSAHSSA AIHKALVKGL EAANLPADAI
     QIVPVTDRAA VGEMLKGLGG AIDVIVPRGG KSLVARVQSE ARVPVFAHLE GICHLYIDKS
     ADLDMARRIA LDAKMRRTGI CGAAETLLVD RAVASTHLAP ILGDLAAGGC EIRGSAEVLA
     LYPAAKPATE EDWSTEYLDA IISVALVDGI SGAIDHINRY SSHHTEAIVA EDAQTVARFF
     NEIDSAILLH NASTQFADGG EFGMGAEIGI ATGKMHARGP VGVEQLTSFK YRVRGSGQVR
     G
//