(data stored in ACNUC7421 zone)

SWISSPROT: PROA_PSEHT

ID   PROA_PSEHT              Reviewed;         415 AA.
AC   Q3IEY7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 87.
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=PSHAa0280;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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}.
DR   EMBL; CR954246; CAI85379.1; -; Genomic_DNA.
DR   RefSeq; WP_011326993.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEY7; -.
DR   SMR; Q3IEY7; -.
DR   STRING; 326442.PSHAa0280; -.
DR   EnsemblBacteria; CAI85379; CAI85379; PSHAa0280.
DR   KEGG; pha:PSHAa0280; -.
DR   PATRIC; fig|326442.8.peg.266; -.
DR   eggNOG; ENOG4105C2S; Bacteria.
DR   eggNOG; COG0014; LUCA.
DR   HOGENOM; HOG000246356; -.
DR   KO; K00147; -.
DR   OMA; CNAIETL; -.
DR   OrthoDB; POG091H00OT; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; 3.40.605.10; -; 2.
DR   HAMAP; MF_00412; ProA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
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; 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;
DR   PRODOM; Q3IEY7.
DR   SWISS-2DPAGE; Q3IEY7.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis; Reference proteome.
FT   CHAIN         1    415       Gamma-glutamyl phosphate reductase.
FT                                /FTId=PRO_0000230013.
SQ   SEQUENCE   415 AA;  44764 MW;  7C2BCB3DFDB8CFA6 CRC64;
     MSLITDISRQ AAKAAHQLAL LDTETKNKVL LDMAAALRAE KAFIIKENES DLAAARDNNL
     AAAMVDRLTL NDERVEAMAE GIEVIVSLDD PVGQLRDITE RPNGIKIRKM RVPLGVVCMI
     YEARPNVTAD AGALCFKSGN SVILRGGKEA LKSSQAIASV MHSVLAKHNL PEALISVIPD
     PDRGLLMELM QQRDSIDLII PRGGEGLINF VTENSTIPVI QHFKGVCHLY VDKDADLEVA
     INLLLNGKTQ RTGVCNALEG LVVHQDIANE FLNLCAVVLR QEGVKINADS QAATYFDNAT
     VLGDDEFGEE YLDLEIAIRV VPSFAAAVEH IAQFGSHHTE VICTKNAATA ELFQRSVDAS
     VVTVNASSRF SDGSQLGLGA EIGIATSKLH AYGPMGLESL TTEKYLVNGD GQIRE
//

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