ID   PROA1_BACLD             Reviewed;         415 AA.
AC   Q65KU7; Q62W94;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 35.
DE   RecName: Full=Gamma-glutamyl phosphate reductase 1;
DE            Short=GPR 1;
DE            EC=1.2.1.41;
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase 1;
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase 1;
DE            Short=GSA dehydrogenase 1;
GN   Name=proA1; OrderedLocusNames=BLi01413, BL03751;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).
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; AE017333; AAU40317.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU22964.1; -; Genomic_DNA.
DR   RefSeq; YP_078602.1; -.
DR   RefSeq; YP_091010.1; -.
DR   GeneID; 3030461; -.
DR   GeneID; 3097972; -.
DR   GenomeReviews; CP000002_GR; BL03751.
DR   GenomeReviews; AE017333_GR; BLi01413.
DR   KEGG; bld:BLi01413; -.
DR   KEGG; bli:BL03751; -.
DR   NMPDR; fig|279010.5.peg.867; -.
DR   HOGENOM; Q65KU7; -.
DR   BioCyc; BLIC279010:BL03751-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 1.
FT                                /FTId=PRO_0000189693.
SQ   SEQUENCE   415 AA;  45473 MW;  473217C94BC4988F CRC64;
     MSEVIEKAKK AKVAKEELVH QPTERKNEAL SFIAEAIRFK QDEILAENEK DIVRGKEKGF
     SPALLDRLAL TPERLNDIAD AVMLLTKLED PVGETLETIR KDNGLFIENV RVPLGVVGMI
     YEARPNVTVD AATLCLKTGN AVILRGSSSA INSNKALVRV IREALERSAL PEDAVQLIED
     TSKETAKQLF TLNDGLDVLI PRGGKNLIDM VVRESTVPVL ETGAGNCHIF IDESAQPDMA
     EQVVINAKTQ RPSVCNAIET VLIHKGWAEE HTKALLQKLE EAGVEIRGDE AVCTMLPSAV
     PARETDWGTE FLAPVVSIKT VAGIDEAIRH IRQYGTRHSE AILTENQENA RYFLTSVDAA
     AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLKAL TSSKYIIKGN GQIRI
//