ID   PROA_AERHH              Reviewed;         417 AA.
AC   A0KNQ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=AHA_3420;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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.
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; CP000462; ABK38804.1; -; Genomic_DNA.
DR   RefSeq; YP_857909.1; -.
DR   GeneID; 4487146; -.
DR   GenomeReviews; CP000462_GR; AHA_3420.
DR   KEGG; aha:AHA_3420; -.
DR   TIGR; AHA_3420; -.
DR   OMA; A0KNQ8; 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; IPR000965; Gglut_pp_reduct.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 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    417       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_1000049932.
SQ   SEQUENCE   417 AA;  44328 MW;  3D9241D61B0E51CF CRC64;
     MSLEKMGQAA REAAYQLATV STAQKNRALA AIADELEARS HQILAANEKD IAAGRAAGLS
     DAMLDRLLLN PARLAGIVAD VRKVISLDDP VGAEIDSRVL ENGLRLSRRR VPIGVIGVIY
     EARPNVTIDI ASLCLKTGNA SILRGGRETF HSNLELVRVI QSALAASGLP RDAVQYIDNP
     DRALVGELLR LDRYVDMIIP RGGAGLHKMC KENSSIPVII GGFGISHIFV DESADLARSL
     AVIDNAKVQR PSACNALDSL LVHEKVAATL LPQLVGLMNE RKVALVATPE AMPLLAGADS
     LRAAGPEDFD TEWLSLTLGV KLVADVNEAL AHMREHNAGH SDAILTNDLA NAERFVNGAG
     SAAVYVNAST RFTDGGQFGL GAEVAVSTQM LHARGPMGLT ELTSYKWVGL ADYLSRA
//