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Database: UniProt
Entry: B7JWV9_CYAP8
LinkDB: B7JWV9_CYAP8
Original site: B7JWV9_CYAP8 
ID   B7JWV9_CYAP8            Unreviewed;       420 AA.
AC   B7JWV9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   28-FEB-2018, entry version 61.
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   OrderedLocusNames=PCC8801_1762 {ECO:0000313|EMBL:ACK65808.1};
OS   Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 /
OS   RF-1)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK65808.1, ECO:0000313|Proteomes:UP000008204};
RN   [1] {ECO:0000313|Proteomes:UP000008204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M.,
RA   Min H., Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a
RT   group of unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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   -!- 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   -!- 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; CP001287; ACK65808.1; -; Genomic_DNA.
DR   RefSeq; WP_012595081.1; NC_011726.1.
DR   ProteinModelPortal; B7JWV9; -.
DR   STRING; 41431.PCC8801_1762; -.
DR   EnsemblBacteria; ACK65808; ACK65808; PCC8801_1762.
DR   KEGG; cyp:PCC8801_1762; -.
DR   eggNOG; ENOG4108ND4; Bacteria.
DR   eggNOG; COG0014; LUCA.
DR   HOGENOM; HOG000246356; -.
DR   KO; K00147; -.
DR   OMA; GNCYLYW; -.
DR   OrthoDB; POG091H00OT; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000008204; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789523};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008204};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
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:ACK65808.1};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008204}.
FT   DOMAIN       14    226       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   420 AA;  46385 MW;  62B0FF30D0A4E93D CRC64;
     MALENSPNLM LTSVQRAYNA FLALATRDSQ ERSQGIRAMA RGIGNAFDDI LEANTLDLEM
     SREMAVPDLL IDWLKLTPER LNALVDLLNR LAEVPDPIQR VFHAPYPLST SQTYCQLMPL
     GVIALIYETF PELGAIAAGF CLKTGNSLIL RGCGSSTHSN AVIANILQAA LEEVKLPKGC
     LEVLSGEEGN SIQDLVTQHQ YLSLVIPYGR PSLVDQVTQL ATAPVLKSAM GNCYLYWSPT
     VDLDLVRWVI VDSHASEPDP VNAIEKVLIS PLQNPSILVR LFNILREKGF QLRGDAELSA
     EFPDYLVPVK PSEWGHPYLD KIIAFKVVND LSEGITWINQ YSNGHADCLV TDSYPESRQF
     AMEVDSALVY INASSRFSRN PKQGESLFLG VSNQKGHHRG LISLETFTTL KQVVQGNGKF
//
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