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MAT1_BEMTA
ID   MAT1_BEMTA              Reviewed;         461 AA.
AC   P0DUQ3; A0A861LVW7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Phenolic glucoside malonyltransferase 1 {ECO:0000303|PubMed:33770502};
DE            Short=BtPMaT1 {ECO:0000303|PubMed:33770502};
DE            EC=2.3.1.- {ECO:0000269|PubMed:33770502};
DE            EC=2.3.1.116 {ECO:0000269|PubMed:33770502};
GN   Name=MAT1 {ECO:0000303|PubMed:33770502};
OS   Bemisia tabaci (Sweetpotato whitefly) (Aleurodes tabaci).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aleyrodoidea;
OC   Aleyrodidae; Aleyrodinae; Bemisia.
OX   NCBI_TaxID=7038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=MED;
RX   PubMed=33770502; DOI=10.1016/j.cell.2021.02.014;
RA   Xia J., Guo Z., Yang Z., Han H., Wang S., Xu H., Yang X., Yang F., Wu Q.,
RA   Xie W., Zhou X., Dermauw W., Turlings T.C.J., Zhang Y.;
RT   "Whitefly hijacks a plant detoxification gene that neutralizes plant
RT   toxins.";
RL   Cell 0:0-0(2021).
CC   -!- FUNCTION: Phenolic glucoside malonyltransferase that neutralizes
CC       phenolic glycosides in host plants (PubMed:33770502). Catalyzes the
CC       transfer of a malonyl group from malonyl-CoA to the phenolic
CC       glycosides, leading to their detoxification (PubMed:33770502). Phenolic
CC       glycosides, which are among the most abundant plant secondary
CC       metabolites, act as plant defense compounds: they strongly affect
CC       growth, development and behavior of insect herbivores
CC       (PubMed:33770502). Has malonyltransferase activity against flavonoids
CC       kaempferol 3-O-glucoside, kaempferol 7-O-glucoside, isoquercetin
CC       (quercetin 3-O-beta-D-glucopyranoside), apigetrin (apigenin 7-O-beta-D-
CC       glucoside) and prunin (naringenin 7-O-beta-D-glucoside)
CC       (PubMed:33770502). Also has activity toward non-flavonoid rhaponticin,
CC       but with lower efficiency (PubMed:33770502).
CC       {ECO:0000269|PubMed:33770502}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a flavonol 3-O-beta-D-glucoside + malonyl-CoA = a flavonol 3-
CC         O-(6-O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:20085,
CC         ChEBI:CHEBI:16816, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:58034; EC=2.3.1.116;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20086;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kaempferol 3-O-beta-D-glucoside + malonyl-CoA = CoA +
CC         kaempferol 3-O-(6-O-malonyl-beta-D-glucoside); Xref=Rhea:RHEA:67336,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:169942,
CC         ChEBI:CHEBI:169943; Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67337;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-CoA + quercetin 3-O-beta-D-glucoside = CoA + quercetin
CC         3-O-(6-O-malonyl-beta-D-glucoside); Xref=Rhea:RHEA:67340,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:144437,
CC         ChEBI:CHEBI:169948; Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67341;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a flavonol 7-O-beta-D-glucoside + malonyl-CoA = a flavonol 7-
CC         O-(6-O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:58796,
CC         ChEBI:CHEBI:52144, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:142805; Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58797;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-naringenin 7-O-beta-D-glucoside + malonyl-CoA = (2S)-
CC         naringenin 7-O-(6-O-malonyl-beta-D-glucoside) + CoA;
CC         Xref=Rhea:RHEA:67356, ChEBI:CHEBI:28327, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:169950;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67357;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kaempferol 7-O-beta-D-glucoside + malonyl-CoA = CoA +
CC         kaempferol 7-O-(6-O-malonyl-beta-D-glucoside); Xref=Rhea:RHEA:67344,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:169944,
CC         ChEBI:CHEBI:169945; Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67345;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apigenin 7-O-beta-D-glucoside + malonyl-CoA = apigenin 7-O-(6-
CC         O-malonyl-beta-D-glucoside) + CoA; Xref=Rhea:RHEA:67348,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:77722,
CC         ChEBI:CHEBI:169949; Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67349;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-CoA + rhaponticin = 6-O-malonyl-rhaponticin + CoA;
CC         Xref=Rhea:RHEA:67352, ChEBI:CHEBI:8824, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:169946;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67353;
CC         Evidence={ECO:0000269|PubMed:33770502};
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues (PubMed:33770502). Most
CC       highly expressed in the abdomen and especially in the gut
CC       (PubMed:33770502). {ECO:0000269|PubMed:33770502}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages with higher
CC       expression in adults (PubMed:33770502). Also detected in the egg stage
CC       to a much lower level (PubMed:33770502). {ECO:0000269|PubMed:33770502}.
CC   -!- MISCELLANEOUS: MAT1 protein-coding gene was acquired from plants
CC       through a plant-to-insect horizontal gene transfer event.
CC       {ECO:0000269|PubMed:33770502}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. Phenolic
CC       glucoside malonyltransferase subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=For the sake of sap - Issue
CC       244 of February 2022;
CC       URL="https://web.expasy.org/spotlight/back_issues/244/";
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DR   EMBL; MN756010; QNN26309.1; -; mRNA.
DR   SMR; P0DUQ3; -.
DR   GO; GO:0047165; F:flavonol-3-O-beta-glucoside O-malonyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0050736; F:O-malonyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0098754; P:detoxification; IDA:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Detoxification; Transferase.
FT   CHAIN           1..461
FT                   /note="Phenolic glucoside malonyltransferase 1"
FT                   /id="PRO_0000453286"
FT   MOTIF           167..171
FT                   /note="HXXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT   MOTIF           400..404
FT                   /note="DFGWG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q589Y0"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   ACT_SITE        400
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   BINDING         281..282
FT                   /ligand="malonyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57384"
FT                   /evidence="ECO:0000250|UniProtKB:Q589Y0"
SQ   SEQUENCE   461 AA;  51733 MW;  6C61394F12DB38DC CRC64;
     MSISSSVAVL NVVQVSPPTA PVNNAFQDRI SLTHFDLLAL RAPPNQRLFF YETHLPISAF
     AETVIPKLRD SLSLTLQNFR PLAGTLIWSL HSDEPYIRIK DDDSVPLTIA ETDADPQKLF
     DDPFQQETDL QQLLPPLRVS ETEASLLALQ ITLFPSGDIC LGITFHHAAQ DGASLALFLK
     SWAHICRHGD DPPLPQNLIP IFDRDFIDDP KNIKQLFLDH LLTPLTPGGP RNRSVKPMEK
     PFNDRMHGSF RLTVDDIENL RRRITSLQVQ NTSQEPPVRM STVVVTCAYV LTCFVKAGLT
     KKHVRFILPA DLRKRLQPPV PDNYYGNCVF GCTVDMSSDD LAGQDGLVVA AKTISSVVSE
     LDANDHRTFF ENFLLNNTIS QEETKVGVGG SIYFSLDEKD FGWGGPKHLK NVPPWPNHIY
     LAERRDGDKG VDFCLMLAKQ EMAEFESKFL DDLKLLEKRS C
 
 
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