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Database: UniProt
Entry: P94872
LinkDB: P94872
Original site: P94872 
ID   PROA_LEPIN              Reviewed;         416 AA.
AC   P94872;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   29-OCT-2014, entry version 115.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000255|HAMAP-Rule:MF_00412};
GN   OrderedLocusNames=LA_0854;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
OS   (strain 56601).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serogroup Icterohaemorrhagiae;
RA   Stamm L.V., Barnes N.Y.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate
CC       5-phosphate into L-glutamate 5-semialdehyde and phosphate. The
CC       product spontaneously undergoes cyclization to form 1-pyrroline-5-
CC       carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000255|HAMAP-
CC       Rule:MF_00412}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00412}.
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DR   EMBL; U73651; AAB39854.1; -; Genomic_DNA.
DR   EMBL; AE010300; AAN48053.1; -; Genomic_DNA.
DR   RefSeq; NP_711035.1; NC_004342.2.
DR   ProteinModelPortal; P94872; -.
DR   STRING; 189518.LA0854; -.
DR   EnsemblBacteria; AAN48053; AAN48053; LA_0854.
DR   GeneID; 1150197; -.
DR   KEGG; lil:LA_0854; -.
DR   PATRIC; 22382562; VBILepInt91350_0858.
DR   eggNOG; COG0014; -.
DR   HOGENOM; HOG000246356; -.
DR   InParanoid; P94872; -.
DR   KO; K00147; -.
DR   OMA; ALTSYKW; -.
DR   OrthoDB; EOG6FFSCX; -.
DR   BioCyc; LINT189518:GJBB-698-MONOMER; -.
DR   UniPathway; UPA00098; UER00360.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   HAMAP; MF_00412; ProA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR000965; G-glutamylP_reductase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; SSF53720; 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; Reference proteome.
FT   CHAIN         1    416       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000189743.
FT   CONFLICT     32     32       V -> I (in Ref. 1; AAB39854).
FT                                {ECO:0000305}.
FT   CONFLICT    299    299       N -> K (in Ref. 1; AAB39854).
FT                                {ECO:0000305}.
FT   CONFLICT    305    305       E -> Q (in Ref. 1; AAB39854).
FT                                {ECO:0000305}.
SQ   SEQUENCE   416 AA;  45768 MW;  A949288589EB0B9A CRC64;
     MKEIEYVQDL CSRAKKASKV LKQLSSSKKN KVLLSLADLL EKRKAEILLA NELDLKDGKE
     KKLSSALMDR LLLNEKRIFS MASAVREIAA LPDPIGEVTR GITLPNGLEL VTRRVPLGVV
     MVIYESRPNV TIDVGALSFK SGNACILRGG SEAFYSNEIL IKLFHEILIK EEIDIGSVVF
     VDKTDRSFMI PFFQQTSLID IVVPRGGEGL IRFVSENSKI PVVKHDKGVC NLYIDQDADP
     EKVIPIVINS KVQRPGVCNS TENLILHNGY PFRKELLEAL AKEGVELLLD PSSLALYPNG
     KPVKEQDYLE EFLDLRLSVK TVSSLEEALA FIEKTSSGHT EAIVTEDLNT ARIFTNSLDS
     AALFINCSTR FHDGGEFGLG AEVGISTGKL HVRGPMGLVH LTTTTTYVTG NGQIRG
//
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