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Database: UniProt
Entry: A0A0Q5TZ51_9SPHI
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ID   A0A0Q5TZ51_9SPHI        Unreviewed;       415 AA.
AC   A0A0Q5TZ51;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-FEB-2018, entry version 17.
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=ASG14_00680 {ECO:0000313|EMBL:KQS41036.1};
OS   Pedobacter sp. Leaf194.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS41036.1, ECO:0000313|Proteomes:UP000051708};
RN   [1] {ECO:0000313|EMBL:KQS41036.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41036.1,
RC   ECO:0000313|Proteomes:UP000051708};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS41036.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41036.1,
RC   ECO:0000313|Proteomes:UP000051708};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KQS41036.1}.
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DR   EMBL; LMPU01000001; KQS41036.1; -; Genomic_DNA.
DR   RefSeq; WP_056869153.1; NZ_LMPU01000001.1.
DR   EnsemblBacteria; KQS41036; KQS41036; ASG14_00680.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000051708; 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; 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.
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:UP000051708};
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};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00412,
KW   ECO:0000256|SAAS:SAAS00789517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051708}.
FT   DOMAIN       36    211       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   COILED        3     23       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   415 AA;  45470 MW;  B60CC0C01FA6C769 CRC64;
     MNYKQYFENA KQASRKLVGL SKETANNVLA DLADALILHT PEILIENEKD LAKMSIEDPK
     HDRLKLTEER IADIVNDVRN VVNLASPLGD ILSDKTLENK LRIQKVRVPL GVVGVIYEAR
     PNVTADVFSL CFKTGNVAVL KGGSDAECSN LAIAKVIKNV LAKHEIDPNV LTLLPAERTA
     TEALLNARGF VDVLIPRGSS SLINYVRDNS KIPVIETGAG IVHTYFDESG DLEKGKAIIF
     NAKTRRVSVC NSLDCVLINR NRLADLPELL APLAGGKVML FADEQSYEKL KPTYPEQLLS
     RATKEHFGTE FLSLKMAVKV VDDFQEGLNH IAEYSSKHSE AIISESAANI TRFLNEVDAA
     AVYANASTGF TDGAQFGLGA EIGISTQKIH ARGPMGLEEL TSYKWVVRGD GQIRR
//
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