ID   PROA_AQUAE              Reviewed;         435 AA.
AC   O67166;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   16-JUN-2009, entry version 65.
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=aq_1071;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07119.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70392; C70392.
DR   RefSeq; NP_213729.1; -.
DR   HSSP; Q9WYC9; 1O20.
DR   GeneID; 1193800; -.
DR   GenomeReviews; AE000657_GR; aq_1071.
DR   KEGG; aae:aq_1071; -.
DR   NMPDR; fig|224324.1.peg.744; -.
DR   HOGENOM; O67166; -.
DR   BioCyc; AAEO224324:AQ_1071-MON; -.
DR   BRENDA; 1.2.1.41; 189781.
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    435       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189684.
SQ   SEQUENCE   435 AA;  49119 MW;  BE6500C58A2B2D61 CRC64;
     MNYIEEKVNR ARSVLRELTS LKTSVKNETL LKVAELIDKN RDYIKEENRK DVEKAKEMGL
     RPAVVDRLVL NDKRIDGMVK VLKDVASLPD PVGEIIKMWN LPNGLKVGRM RVPLGVIFIV
     YESRPNVTIE ASSLCMKSSN AVILRGGKEA INSNKALVNL IKEACRETGF PEDAVQFIDR
     SEREIVWEIL KMEGKIDVAI PRGGESLIRA VVEHAKVPVI KHYKGVCNIY VDDEADLEKA
     YHIVYNAKVQ RPSVCNAVEN LVINRKILKE FFPKMAYYLG KAGVELRCDE ESLQVIKENP
     KLSFVNAKPA TEEDYYEEFL DLILAVKVVD DVDEAIAFIE KYGSKHSDAI ITENYTKAMK
     FLREVDSAAV YVNASTRFTD GNEFGLGAEM GISTDKIHAR GPMALEELTI PKFVILGEGQ
     VRDNFGVPEE WMKEF
//