ID   PROA_ALHEH              Reviewed;         420 AA.
AC   Q0ABN0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Mlg_0403;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI55757.1; -; Genomic_DNA.
DR   RefSeq; YP_741247.1; -.
DR   GeneID; 4269981; -.
DR   GenomeReviews; CP000453_GR; Mlg_0403.
DR   KEGG; aeh:Mlg_0403; -.
DR   NMPDR; fig|187272.6.peg.381; -.
DR   HOGENOM; Q0ABN0; -.
DR   OMA; Q0ABN0; 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    420       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000340870.
SQ   SEQUENCE   420 AA;  45465 MW;  A74B5C5EE21FC49A CRC64;
     MTEDIRAYMQ TLGRQAREAA REMARADTGH KNAALHAMAD ALEEHAGDLK RANADDLENG
     RANNLDPALL DRLELNDERI HGMAEGLRQI AALPDPVGAI RDLAFRPSGI QVGRMRVPLG
     VIGIIYESRP NVTADAAALC LKSGNAAILR GGSEARHSNA AIAACVRAGL KRAGLPGEAV
     QVVETTDRAA VGELIRMDEY VDVLVPRGGK GLIERITAEA TVPVIKHLDG ICHVYIDDSA
     DPAKAISVAY NAKTQRLGTC NTMETLLVAE AIAERVLPEL ARRYRESEVE LRGCEATRRL
     IPDAVPATKE DWSTEYLDAI VSIRIVPGLD EAIEHIARHS SGHTESILTE DWSRARRFLR
     EVDSSSVMVN ASTRFADGFE YGLGAEIGIS TDKLHARGPV GLEGLTTEKF IVLGDGHIRE
//