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Database: UniProt
Entry: B7S326_9GAMM
LinkDB: B7S326_9GAMM
Original site: B7S326_9GAMM 
ID   B7S326_9GAMM            Unreviewed;       418 AA.
AC   B7S326;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   28-FEB-2018, entry version 60.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000256|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000256|HAMAP-Rule:MF_00412,
GN   ECO:0000313|EMBL:EEB76918.1};
GN   ORFNames=GPB2148_222 {ECO:0000313|EMBL:EEB76918.1};
OS   marine gamma proteobacterium HTCC2148.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Halieaceae.
OX   NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB76918.1, ECO:0000313|Proteomes:UP000002793};
RN   [1] {ECO:0000313|Proteomes:UP000002793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX   PubMed=20472793; DOI=10.1128/JB.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
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:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00806217}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
CC       NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000256|HAMAP-
CC       Rule:MF_00412, ECO:0000256|SAAS:SAAS00789550}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00412, ECO:0000256|SAAS:SAAS00789481}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00806220}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00412,
CC       ECO:0000256|SAAS:SAAS00750599}.
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DR   EMBL; DS999243; EEB76918.1; -; Genomic_DNA.
DR   RefSeq; WP_007230775.1; NZ_DS999243.1.
DR   ProteinModelPortal; B7S326; -.
DR   STRING; 247634.GPB2148_222; -.
DR   EnsemblBacteria; EEB76918; EEB76918; GPB2148_222.
DR   eggNOG; ENOG4105C2S; Bacteria.
DR   eggNOG; COG0014; LUCA.
DR   OrthoDB; POG091H00OT; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000002793; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
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; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   InterPro; IPR000965; GPR_dom.
DR   Pfam; PF00171; Aldedh; 2.
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 {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789523}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002793};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00806221};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00412, ECO:0000256|SAAS:SAAS00789553};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789546, ECO:0000313|EMBL:EEB76918.1};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002793}.
FT   DOMAIN       12    282       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   DOMAIN      309    374       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   COILED       33     53       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   418 AA;  44535 MW;  B523F417E8762FDA CRC64;
     MEVEQYMVEL GRKARAASRE VAASATSARN AALLAARDAL DSARAELAAA NTTDLERGAA
     NGLDAPLMDR LELTPARIDT MLEGLTQVAN LPDPVGSITD MNTMPSGIQV GRMRVPLGVI
     GIIYESRPNV TVEAASLCLK SGNATILRGG SEALESNMAI ARCLTMGLEH AGLPAAAVQV
     VATRDRAAVG QLITMPQYVD VIVPRGGKGL IERISNDAKV PVIKHLDGTC HVYIDDGADE
     DMAEAIAVNA KTQRYGTCNT METLLVHADM ASVMLPRLGE AYGAAGVELR GCERTMAILP
     GVTAASEDDW YQEYLGPILA VRVVEDLEQA MDHINTYSSQ HTESIVTRDH GRAMRFLREV
     DSSSVMVNAS TRFADGFEYG LGAEIGISTD KLHARGPVGL EGLTSVKYIV LGEGQVRN
//
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