ID   PROA_BACA2              Reviewed;         415 AA.
AC   A7Z3T1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
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=RBAM_012940;
OS   Bacillus amyloliquefaciens (strain FZB42).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS73657.1; -; Genomic_DNA.
DR   RefSeq; YP_001420888.1; -.
DR   GeneID; 5460434; -.
DR   GenomeReviews; CP000560_GR; RBAM_012940.
DR   KEGG; bay:RBAM_012940; -.
DR   OMA; A7Z3T1; QYPAACN.
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    415       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_1000049935.
SQ   SEQUENCE   415 AA;  45134 MW;  36FC30E6672872D9 CRC64;
     MSEVLQKAAL AKEAAAEMVM KTTAEKNEAL QCIADGLRNE RRLILTENQK DIEAGRNRGL
     TPDIIDRLTL DEKRLLDIAD AVELLIGLED PVGESLETIQ KENGLSIEKI RVPLGVVGMI
     YEARPNVTVD AATLCLKTGN AVVLRGSSSA IHSNIALVSV MKRALGLSKL PIDAVQLIED
     TSKETAKQLF TLNDGLDVLI PRGGKNLIDL VVRESTVPVL ETGAGNCHVY IDESADPQMA
     SEVVINAKTQ RPSVCNAIES LLIHEKWAEE HGRKLLNQLT EKGVELRGDQ VICRLEPQAK
     QAEEADWGAE YLAPILSVKT VQDVQEAVRH IQQYGTNHSE AILTENAEHA AYFQTAVDAA
     AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLPAL TSTKIIIKGN GQIRV
//