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 01-MAY-2013, entry version 107.
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=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-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 (By similarity).
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; 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 KO; K00147; -.
DR OMA; SIISEHQ; -.
DR ProtClustDB; PRK00197; -.
DR BioCyc; LINT189518:GJBB-698-MONOMER; -.
DR UniPathway; UPA00098; UER00360.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA: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 PANTHER; PTHR11063:SF1; PTHR11063:SF1; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF000151; GPR; 1.
DR SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 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 CONFLICT 299 299 N -> K (in Ref. 1; AAB39854).
FT CONFLICT 305 305 E -> Q (in Ref. 1; AAB39854).
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
//
