ID   PROA_BACSK              Reviewed;         415 AA.
AC   Q5WH54;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-NOV-2008, entry version 31.
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=ABC1766;
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) 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.
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; AP006627; BAD64301.1; -; Genomic_DNA.
DR   RefSeq; YP_175262.1; -.
DR   GeneID; 3202777; -.
DR   GenomeReviews; AP006627_GR; ABC1766.
DR   KEGG; bcl:ABC1766; -.
DR   NMPDR; fig|66692.3.peg.1714; -.
DR   HOGENOM; Q5WH54; -.
DR   BioCyc; BCLA66692:ABC1766-MON; -.
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   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_0000189695.
SQ   SEQUENCE   415 AA;  44511 MW;  A15EECC7BAB0DCA7 CRC64;
     MATAKLISQK AKAHAPSLSQ ATTAEKNSVL QAMAQQLKAD ADVLLQANQL DIANAKKNGL
     SDHLIDRLLL TKARIDAMAT AIDHLIELPE PIGAVKEEIK RPNGLVIKEM VVPFGVVGMI
     YEARPNVTVD ACTLAVKTGN AVVLRGSASA LHSNKAIVHT LKKAFQNSPI HPDVIQLLED
     TSKEEAANMM QLKSTIDVLI PRGGANLIQT VLQEATIPVI ETGVGNCHVY VASSADPDMA
     FDIVVNAKTQ RPSVCNACET LLVEQSFAKA HLPALVERLS AKGVSLVGNE GACTLDPRIA
     QANEDDWSTE YLDLRLAIRV VADTNEAIAH INQYGTKHSE AIITESLAER DTFFATVDAA
     CVYHNASTRF TDGFEFGFGA EIGISTQKLH ARGPMGLKAL TTSKYGIYGE GQVKE
//