ID PROA_BACA2 Reviewed; 415 AA.
AC A7Z3T1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 01-MAY-2013, entry version 51.
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=RBAM_012940;
OS Bacillus amyloliquefaciens (strain FZB42).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant
RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73657.1; -; Genomic_DNA.
DR RefSeq; YP_001420888.1; NC_009725.1.
DR ProteinModelPortal; A7Z3T1; -.
DR STRING; 326423.RBAM_012940; -.
DR EnsemblBacteria; ABS73657; ABS73657; RBAM_012940.
DR GeneID; 5460434; -.
DR KEGG; bay:RBAM_012940; -.
DR PATRIC; 18747613; VBIBacAmy31356_1283.
DR eggNOG; COG0014; -.
DR HOGENOM; HOG000246356; -.
DR KO; K00147; -.
DR OMA; EVGISTQ; -.
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 1 415 Gamma-glutamyl phosphate reductase.
FT /FTId=PRO_1000049935.
SQ SEQUENCE 415 AA; 45134 MW; 36FC30E6672872D9 CRC64;
MSEVLQKAAL AKEAAAEMVM KTTAEKNEAL QCIADGLRNE RRLILTENQK DIEAGRNRGL
TPDIIDRLTL DEKRLLDIAD AVELLIGLED PVGESLETIQ KENGLSIEKI RVPLGVVGMI
YEARPNVTVD AATLCLKTGN AVVLRGSSSA IHSNIALVSV MKRALGLSKL PIDAVQLIED
TSKETAKQLF TLNDGLDVLI PRGGKNLIDL VVRESTVPVL ETGAGNCHVY IDESADPQMA
SEVVINAKTQ RPSVCNAIES LLIHEKWAEE HGRKLLNQLT EKGVELRGDQ VICRLEPQAK
QAEEADWGAE YLAPILSVKT VQDVQEAVRH IQQYGTNHSE AILTENAEHA AYFQTAVDAA
AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLPAL TSTKIIIKGN GQIRV
//
