ID   PROA_BORPA              Reviewed;         419 AA.
AC   Q7W9M7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-NOV-2008, entry version 41.
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=BPP1728;
OS   Bordetella parapertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640428; CAE37029.1; -; Genomic_DNA.
DR   RefSeq; NP_884003.1; -.
DR   GeneID; 1667047; -.
DR   GenomeReviews; BX470249_GR; BPP1728.
DR   KEGG; bpa:BPP1728; -.
DR   NMPDR; fig|257311.1.peg.1637; -.
DR   HOGENOM; Q7W9M7; -.
DR   BioCyc; BPAR257311:BPP1728-MON; -.
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; IPR015590; Aldehyde_DHase.
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   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_0000189702.
SQ   SEQUENCE   419 AA;  44321 MW;  B636D8727080BDEF CRC64;
     MSSIETYMQS VGEQTRTASR AMMRATGAAK NQALLAMAEA ILAQRAELQA ANAKDVAAAR
     ANGLEAALLD RLTLSDRSIA LMAEGLRQIA ALPDPVGSIT ATSVRPNGMR VAQMRVPLGV
     IGIIYESRPN VTIDAAALCL KSGNATILRG GSEALHSNVA LGRIVQAGLQ AAGLPTAAVQ
     VIDTTDRAAV GKLVTMTEHV DVIVPRGGKG LISRLAQEAR VPLIKHLDGN CHVYVDAAAD
     LAKAHDIAFN AKTYRYGVCG AMETLLVHAD VAQRLLPVLG QALHEHGVEL RGCARALQWL
     PEGKPADDAD WATEYLGPIL AVRVVDTIDE AMDHIARWGS GHTDAIVTEN LSAAQRFQRE
     VDSSSVYVNL PTCFADGFEY GLGAEIGIST NRLHARGPVG LEGLTTLKWV LNGEGQVRG
//