ID   PROA_BIFAA              Reviewed;         427 AA.
AC   A1A1U9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BAD_0901;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S.,
RA   Hirai S., Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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 (By similarity).
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; AP009256; BAF39682.1; -; Genomic_DNA.
DR   RefSeq; YP_909764.1; -.
DR   GeneID; 4556586; -.
DR   GenomeReviews; AP009256_GR; BAD_0901.
DR   KEGG; bad:BAD_0901; -.
DR   NMPDR; fig|1680.3.peg.1171; -.
DR   OMA; A1A1U9; FDTEWLD.
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; IPR015590; Aldehyde_DH.
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   Pfam; PF00171; Aldedh; 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    427       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000340873.
SQ   SEQUENCE   427 AA;  45480 MW;  3DF4BACCB17513E4 CRC64;
     MNADVFEAVC AMGDAARTAQ SQLAQANTEA KNQLLNAIAD ALDQHADDIA AANTLDMNKA
     ETDGMDAGKL DRLKFDQQRI TAAAQGVRHV ASLPDPIGEI VRGYHLENGL RLQQVRVPIG
     VLGMIYEARP NVTVDVASLC IKSGNAVLLR GGHAAEHTNA ATLAVIADVL TKHGYDHNMI
     ATVDQYGRDG ATAMMEARGH IDVLIPRGGA GLIQAVVRNS KVPVIETGAG NVHIYVDRTG
     NPDKAIPILI NAKTQRVGVC NATEKLLVHK DIAESFLPKA AAALAAAGVE MHADERAYGI
     IEHAGIANAQ LVHATDEDWD TEYLALKIGI KVVDSLDEAI AHINRHSTGH TESIIAEDYS
     AIEEFTARID SAVVMVNAST RFTDGGVFGF GAELGISTQK MHARGPMGLH EMTTTKWIGY
     GTGQVRE
//