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Database: UniProt
Entry: M1FCM1_9ALTE
LinkDB: M1FCM1_9ALTE
Original site: M1FCM1_9ALTE 
ID   M1FCM1_9ALTE            Unreviewed;       431 AA.
AC   M1FCM1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   28-FEB-2018, entry version 38.
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   ORFNames=MRBBS_0801 {ECO:0000313|EMBL:AFP29739.1};
OS   Marinobacter sp. BSs20148.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=490759 {ECO:0000313|EMBL:AFP29739.1, ECO:0000313|Proteomes:UP000011757};
RN   [1] {ECO:0000313|EMBL:AFP29739.1, ECO:0000313|Proteomes:UP000011757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20148 {ECO:0000313|EMBL:AFP29739.1};
RX   PubMed=23682144;
RA   Song L., Ren L., Li X., Yu D., Yu Y., Wang X., Liu G.;
RT   "Complete Genome Sequence of Marinobacter sp. BSs20148.";
RL   Genome Announc. 1:E00236-13(2013).
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; CP003735; AFP29739.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFP29739; AFP29739; MRBBS_0801.
DR   KEGG; mbs:MRBBS_0801; -.
DR   PATRIC; fig|490759.3.peg.796; -.
DR   KO; K00147; -.
DR   OrthoDB; POG091H00OT; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000011757; 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; 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;
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:UP000011757};
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};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011757}.
FT   DOMAIN       20    294       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   COILED       46     66       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   431 AA;  45733 MW;  FEB55419802D3868 CRC64;
     MALATSGFKG NKRMDIAAYM NEVGAQARAA AKHVARSTTA VRNQALLAMA QALDAARDEL
     AKANQQDLSA AKASGLDSAM LDRLELTPAR VDAMIEGLLQ VAGLADPIGA ITDMAYRPSG
     IQVGKMRVPL GVIGIIYESR PNVTVEAASL CLKSGNAAIL RGGSESIHSN QAIARCIASG
     LAQAGLPETA VQVIATADRA AVGELITMPQ YVDVIVPRGG KGLIERVSRD ARVPVIKHLD
     GVCHVYIDSH ADPEKALAVA VNAKTQRYGT CNTMETLLVD EEIAADMLPL LNAAFVEKGV
     ELRGCERSRE IVSEMTPATE ADWEAEYLAP ILAIKIVDGL DGAIAHISQF SSRHTDSIVT
     ENYTRARRFL TEVDSSSVMV NASTRFADGF EYGLGAEIGI STDKIHARGP VGLEGLTSQK
     YVVFGDGHIR V
//
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