ID   PROA_AZOSB              Reviewed;         419 AA.
AC   A1KAH8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=azo3218;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95834.1; -; Genomic_DNA.
DR   RefSeq; YP_934720.1; -.
DR   GeneID; 4609012; -.
DR   GenomeReviews; AM406670_GR; azo3218.
DR   KEGG; azo:azo3218; -.
DR   OMA; A1KAH8; 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    419       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000340871.
SQ   SEQUENCE   419 AA;  44257 MW;  28F270332CA1E276 CRC64;
     MQTVGREARA ASRTLAAAST DAKNSALVAM AQAIRDSRDA LLAANAADLA EARAAGLDEA
     LIDRLTLSAK GVEGMAAGLE QVAALPDPVG EITDVKRRPS GIQVGKMRVP LGVVGIIYEA
     RPNVTADAAA LCLKSGNAAI LRGGKEALRS NQAIASCVRT GLAAAGLPQT AVQVLETTDR
     AAVGALITMP EFVDVIVPRG GKGLIERISS EARVPVIKHL DGNCHVYVDD HADPAKVLPI
     VENAKTQRYG TCNTTESLLV ARAVAPRFLS DIGRMLAARN VEMRACPEAL ALLREAGIEG
     ARLSPATEQD WHEEYLAPII AIRVVAGLDE AIAHINTYSS GHTEAILTEH YTHAMRFLRE
     VDSASVMVNA STRFADGFEY GLGAEIGIST DKIHARGPVG LEGLTSQKWI VFGNGEIRR
//