ID   PROA_ACTSZ              Reviewed;         416 AA.
AC   A6VMV2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-NOV-2008, entry version 13.
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=Asuc_0931;
OS   Actinobacillus succinogenes (strain ATCC 55618 / 130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C.,
RA   Richardson P.;
RT   "Complete sequence of Actinobacillus succinogenes 130Z.";
RL   Submitted (JUN-2007) 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; CP000746; ABR74299.1; -; Genomic_DNA.
DR   RefSeq; YP_001344234.1; -.
DR   GeneID; 5348169; -.
DR   GenomeReviews; CP000746_GR; Asuc_0931.
DR   KEGG; asu:Asuc_0931; -.
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; 2.
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    416       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_1000072277.
SQ   SEQUENCE   416 AA;  45186 MW;  D11013433856BC4E CRC64;
     MTNLEVMGKA ARQAAFELSQ LSAGDKNYAL QMIAEQLESQ QQQILAANAR DIDEARINGL
     NDAIIDRLLL TPERLRGIAN DVRHVISLAD PVGKLIDGGI LDSGLKLERI RVPVGVIGTI
     YEARPNVTID VASLCLKTGN AVILRGGKET RHSNRILVEV VQNALEKAGL PKTAVQAITD
     PDRALVMELL KLDRYVDMII PRGGAGLHAL CKQHATIPVI IGGIGVCHTF VEQSADQNRA
     ISVIKNAKTQ RPSTCNTLET LLIQESIAHE FLPKLAAELP VKYYADKTAY SILHHAGAEV
     LAVTEDDLRK EWLCTNLNVV IVQDIEAAVA HIREYGSQHS EAILTESLQL ARRFVAQVDS
     AAVYVNASTR FTDGGQFGLG AEVAVSTQKL HARGPMGLEA LTTYKWVATG DYTVRS
//