ID   PROA_CAMJE              Reviewed;         410 AA.
AC   P53000; Q0PAV8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-NOV-2008, entry version 63.
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=Cj0558c;
OS   Campylobacter jejuni.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX   MEDLINE=93341456; PubMed=8341262; DOI=10.1007/BF00276880;
RA   Louie H., Chan V.L.;
RT   "Cloning and characterization of the gamma-glutamyl phosphate
RT   reductase gene of Campylobacter jejuni.";
RL   Mol. Gen. Genet. 240:29-35(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11168 / Serotype O:2;
RX   MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; M74579; AAA23030.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL34704.1; -; Genomic_DNA.
DR   PIR; F81402; F81402.
DR   PIR; S35213; S35213.
DR   HSSP; Q9WYC9; 1O20.
DR   GenomeReviews; AL111168_GR; Cj0558c.
DR   KEGG; cje:Cj0558c; -.
DR   HOGENOM; P53000; -.
DR   BioCyc; CJEJ192222:CJ0558C-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; 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   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    410       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189710.
FT   CONFLICT     57     57       A -> K (in Ref. 1; AAA23030).
FT   CONFLICT    100    100       S -> N (in Ref. 1; AAA23030).
FT   CONFLICT    104    104       M -> I (in Ref. 1; AAA23030).
FT   CONFLICT    283    283       A -> T (in Ref. 1; AAA23030).
FT   CONFLICT    293    293       K -> E (in Ref. 1; AAA23030).
SQ   SEQUENCE   410 AA;  46000 MW;  EB27A90652906668 CRC64;
     MRNLLENIKK NSQKLLNLTP KDKEKIILKL AQILRENFKI ILEANKKDMA NFTKSGAMKD
     RLLLDEKRIL ALCEGLEKIA YIEDPIGKIS KGWKNYAGLS IQKMSIPLGL ICVIYEARPS
     LSAEIAALMI KSSNACVFKG GSEAKFTNEA IFTLVNKVLK EFDLQDCFAM FTQRDEILQI
     LAFDDLIDVI IPRGSSNMIQ EIANNTKIPL IKQNKGLCHA FVDQSANLDM ALKIILNAKC
     QRVSVCNALE TLLIHEKIAK NFISLLIPEF EKFKVKIHAH ENALAYFNNS NLKIFKANEN
     TFDTEWLDFA LSVKLVKDCD EAIEHINKHS SLHSETIISN DASNIAKFQR LINSSCIYAN
     ASTRFSDGGE FGFGGEVGIS TSKLHARGPM GIEDICTYKY IINGEGQIRE
//