ID   PROA_CHRSD              Reviewed;         428 AA.
AC   Q1QXB4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Csal_1541;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-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.
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; CP000285; ABE58894.1; -; Genomic_DNA.
DR   RefSeq; YP_573593.1; -.
DR   GeneID; 4027639; -.
DR   GenomeReviews; CP000285_GR; Csal_1541.
DR   KEGG; csa:Csal_1541; -.
DR   NMPDR; fig|290398.4.peg.2596; -.
DR   HOGENOM; Q1QXB4; -.
DR   OMA; Q1QXB4; QYPAACN.
DR   BioCyc; CSAL290398:CSAL_1541-MON; -.
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    428       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000252568.
SQ   SEQUENCE   428 AA;  45827 MW;  0CDA35B24B1C3070 CRC64;
     MALETSAPEI ADVEAYMRAL GERARDASRM LARATTAQKN RALHAMAEAL DAARETLETA
     NRRDLEAGRA NGLDEALLDR LALTPARIDS MIEGLRQVAA LPDPVGEIRD MRYLPSGIQV
     GKMRVALGVV GIVYESRPNV TVDAASLCLK SGNATILRGG SEAIQSNRAI ADCIRQGLAA
     ADLDAACVQV VATTDRAAVG ALIAMPEYVD VIVPRGGKGL IERISRDARV PVIKHLDGVC
     HVYVDRAADD AKAVAIADNA KTQRYSPCNT METLLVHVDA APRVLPELAR LYASKGVELR
     ACERARAWLA DAVAATEDDW HAEYLAPILA VRVVDSLEEA IAHINTYGSH HTDAIVTESV
     TDARRFLAEV DSSSVMVNAS TRFADGFEYG LGAEIGISTD KLHARGPVGL EGLTSEKYIV
     YGDGHVRS
//