ID   PROA_CHLAA              Reviewed;         422 AA.
AC   A9WBM7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 14.
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=Caur_1616;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexales; Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Pierson B.K.,
RA   Blankenship R.E., Richardson P.;
RT   "Complete sequence of Chloroflexus aurantiacus J-10-fl.";
RL   Submitted (DEC-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 (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; CP000909; ABY34834.1; -; Genomic_DNA.
DR   RefSeq; YP_001635223.1; -.
DR   GeneID; 5826062; -.
DR   GenomeReviews; CP000909_GR; Caur_1616.
DR   KEGG; cau:Caur_1616; -.
DR   OMA; A9WBM7; QYPAACN.
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    422       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000340877.
SQ   SEQUENCE   422 AA;  44515 MW;  68BC84715CCE3378 CRC64;
     MVDLEAIGRR AKTAARALAK LSTEQKNAAL CAIADGLLAR QDKILAANAA DVADAEKGGT
     PPAIVDRMLL TPARLAAIAG DCRQVASLPD PVGEIFDRRE LPSGLRLYKR RVPIGVIGAI
     YEARPNVTVD IASLCLKAGN AVILRGGSDI ARSVAATTEV IALALEQAGL PAFAVQSIID
     PDRELVRQLL RLDRYVDMII PRGGAGLHRF CVENATVPVI VGGMGVSHIY VEPSADFARA
     VPVIVNAKVQ RPGACNALDT LLVHRAAAST FLPLVAAALA QHGVELRCDL EALAILADAP
     GHEAWNLKPA SPTDFGCEFL ALIVAIKIVG SIDEALDHIA LYGGHSEAIL TGDPISAERF
     TREVDATAVF VNASTRFNDG GQFGLGAEVA ISTNRLHARG PMGLQELTTY TWIGEGDYLV
     RA
//