ID PROA_XANCB Reviewed; 414 AA.
AC B0RS59;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 01-MAY-2013, entry version 49.
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=xcc-b100_1941;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J.,
RA Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A.,
RA Niehaus K., Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use
RT for the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP51294.1; -; Genomic_DNA.
DR RefSeq; YP_001903346.1; NC_010688.1.
DR ProteinModelPortal; B0RS59; -.
DR STRING; 509169.xccb100_1941; -.
DR EnsemblBacteria; CAP51294; CAP51294; xcc-b100_1941.
DR GeneID; 6322087; -.
DR KEGG; xca:xccb100_1941; -.
DR PATRIC; 24083763; VBIXanCam108527_1979.
DR eggNOG; COG0014; -.
DR KO; K00147; -.
DR OMA; QRPNGMT; -.
DR ProtClustDB; PRK00197; -.
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.
FT CHAIN 1 414 Gamma-glutamyl phosphate reductase.
FT /FTId=PRO_1000193675.
SQ SEQUENCE 414 AA; 44171 MW; 5090AC8DC48358E6 CRC64;
MTIKTLALQC RDAAHVLSQL SSSAKQALLE AMAAALEHDG AVILAANARD LEAAREKGVG
TAMLDRLALD TKRLDGIAAA LREVAQLPDP VGQITREDVR PNGIVVQKVR VPLGVIAMIY
EARPNVTADA AALCIKAGNG VILRGGSEAI HSNTAIARAL QSALREANVP EAALTLVEDL
RRETMLELLQ LSDIVDLAIP RGGEGLIRFV AEHARVPVIK HYKGVCHLFV DASADVDLAV
RLLVDGKASR PSACNSLETL LVHADIAERF LPAAAHALRE RHVELRGDAA TRALLPDIAA
ASDEDYAAEF LDLILAIRVV PDLDTALTHI RQYGSDHTEV IATQDTANAE QFVQSLRSAV
VMVNASSRFS DGGELGLGAE IGISTTRLHS YGPMGLEALT VERFVVRGEG QVRH
//
