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Entry: A0A0N0TQI0_9PSEU
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ID   A0A0N0TQI0_9PSEU        Unreviewed;       418 AA.
AC   A0A0N0TQI0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ADK67_31320 {ECO:0000313|EMBL:KOX20050.1};
OS   Saccharothrix sp. NRRL B-16348.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX20050.1, ECO:0000313|Proteomes:UP000037722};
RN   [1] {ECO:0000313|EMBL:KOX20050.1, ECO:0000313|Proteomes:UP000037722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX20050.1,
RC   ECO:0000313|Proteomes:UP000037722};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-
CC       phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC       spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
CC       {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC         glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00000979, ECO:0000256|HAMAP-
CC         Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00412}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOX20050.1}.
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DR   EMBL; LGED01000220; KOX20050.1; -; Genomic_DNA.
DR   RefSeq; WP_053720138.1; NZ_LGED01000220.1.
DR   AlphaFoldDB; A0A0N0TQI0; -.
DR   STRING; 1415542.ADK67_31320; -.
DR   PATRIC; fig|1415542.3.peg.6744; -.
DR   OrthoDB; 9809970at2; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000037722; 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   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   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00412}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00412};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00412};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00412};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW   Rule:MF_00412}.
FT   DOMAIN          110..280
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   418 AA;  43479 MW;  32E94242F0C16C76 CRC64;
     MTEQLLSSAR AALHAAPPVG DPAYRRYCGA LAEHLTSSWP LVLKANEEDV AAARRRGLPP
     VLVERLRLTE DHLDGLLRLI DAVTAELGPA TTPAPPVPIG DWGALRKVPK PLGVVFMVYE
     ARPTVTVEGA LIPVVAGNSV LLRGGKEMAA TDEALATAVH GALVSAGLPA GLVTVIEDPD
     RSVFRALLRR PDAVDVLIPR GSPALIDFCR SAGSIPVIAS GGGVNHLYVH GSADLARAAA
     IALDSKLAEP SACNTLELVL VDEHVADDFV AEVVRTGADV TLKLGGGLKA EPGGGVRIAE
     LASHDLGREF LEPTIGVLPV PDVDAAVEHV RRYGSAHTEG VVSADDAAIE RFTRGVDAAA
     VVVNGSLRLH DGPTLGLGSE ISISTGRLHV RGPVTVSALL THTWVVEARG ALRAERGN
//
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