ID   PROA_ARCB4              Reviewed;         412 AA.
AC   A8EVN0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-NOV-2008, entry version 13.
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=Abu_1757;
OS   Arcobacter butzleri (strain RM4018).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Arcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G.,
RA   Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the
RT   Epsilonproteobacterium Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV68003.1; -; Genomic_DNA.
DR   RefSeq; YP_001490673.1; -.
DR   GeneID; 5624120; -.
DR   GenomeReviews; CP000361_GR; Abu_1757.
DR   KEGG; abu:Abu_1757; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP 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_DHase_C.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DHase.
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    412       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_1000060837.
SQ   SEQUENCE   412 AA;  45081 MW;  1DB0933298630615 CRC64;
     MQEFLQEAKN SSRIIANLGS AQKNRVLNEM ADALIEHSSF ILSHNQKDMN DAKLNNLNDA
     LQDRLLLTEK RIQDMAIAIR QIASQQDPLG KILNGWVTKD GLNIQKVSIP IGVIGIIYES
     RPNVTSDTAA LCFKSGNVCV LKGGKEAENS NKAIATILRE VLRKNNLPEY AISLLPDSSR
     EGVAKLIKQD KYVDLIVPRG GEALIRFVSE NSSIPVIKHD KGICHIFIDQ DANITKIFDI
     VVNAKCQKPS ACNSIETLLI HTNIAALILS GLVETLSLHG TILKGCPETL QHINAIPATL
     EDFDTEYLAN VLNIKIVANV DEAITHIQRH GSGHSESILS ENYTTINKFL SEVDAACVYA
     NASTRFTDGG EFGLGAEVGI STNKLHSRGP MGIEDLTTFK YKIYGQGQIR KG
//