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5MAT1_SALSN
ID   5MAT1_SALSN             Reviewed;         462 AA.
AC   Q8W1W9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Malonyl-coenzyme:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase {ECO:0000303|PubMed:11598135};
DE            Short=Malonyl CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase {ECO:0000312|EMBL:AAL50566.1};
DE            Short=Ss5MaT1 {ECO:0000303|PubMed:11598135};
DE            EC=2.3.1.172;
GN   Name=5MAT1 {ECO:0000303|PubMed:11598135};
OS   Salvia splendens (Scarlet sage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC   Salvia; Salvia subgen. Calosphace; core Calosphace.
OX   NCBI_TaxID=180675;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL50566.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Petal {ECO:0000269|PubMed:11598135};
RX   PubMed=11598135; DOI=10.1074/jbc.m108444200;
RA   Suzuki H., Nakayama T., Yonekura-Sakakibara K., Fukui Y., Nakamura N.,
RA   Nakao M., Tanaka Y., Yamaguchi M.A., Kusumi T., Nishino T.;
RT   "Malonyl-CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase from
RT   scarlet sage (Salvia splendens) flowers. Enzyme purification, gene cloning,
RT   expression, and characterization.";
RL   J. Biol. Chem. 276:49013-49019(2001).
RN   [2] {ECO:0000305}
RP   MUTAGENESIS OF TYR-45; GLN-150; HIS-166; HIS-167; CYS-168; ASP-171;
RP   LYS-258; ARG-301; ASN-315 AND ASP-390, PROPOSED ENZYME MECHANISM, AND
RP   ACTIVE SITES.
RX   PubMed=12578391; DOI=10.1021/bi020618g;
RA   Suzuki H., Nakayama T., Nishino T.;
RT   "Proposed mechanism and functional amino acid residues of malonyl-
RT   CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase from flowers of
RT   Salvia splendens, a member of the versatile plant acyltransferase family.";
RL   Biochemistry 42:1764-1771(2003).
CC   -!- FUNCTION: Catalyzes the transfer of a malonyl group from malonyl-CoA to
CC       the 6'''-hydroxyl group of the 5-glucosyl moiety of anthocyanins.
CC       Active towards bisdemalonylsalvianin (pelargonidin 3-O-(6-caffeoyl-
CC       beta-D-glucoside) 5-O-beta-D-glucoside) and shisonin, but not towards
CC       nodemalonylsalvianin, salvianin, pelargonidin 3,5-diglucoside and
CC       delphinidin 3,5-diglucoside. {ECO:0000269|PubMed:11598135}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-CoA + pelargonidin 3-O-(6-O-[(E)-caffeoyl]-beta-D-
CC         glucoside) 5-O-beta-D-glucoside = 4'''-demalonylsalvianin + CoA;
CC         Xref=Rhea:RHEA:21988, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:58638, ChEBI:CHEBI:58640; EC=2.3.1.172;
CC         Evidence={ECO:0000269|PubMed:11598135};
CC   -!- ACTIVITY REGULATION: Completely inhibited by 10 mM p-coumaric acid,
CC       this inhibition is rapid, reversible and non-competitive. Completely
CC       inhibited by 0.1 mM Cu(2+), 0.1 mM Hg(2+) and 10 mM caffeic acid.
CC       Partially inhibited by 5 mM N-ethylmaleimide, 1 mM diethylpyrocarbonate
CC       and 1 mM acetyl-CoA. {ECO:0000269|PubMed:11598135}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=101.0 uM for bisdemalonylsalvianin (with malonyl-CoA as
CC         cosubstrate) {ECO:0000269|PubMed:11598135};
CC         KM=40.2 uM for shisonin (with malonyl-CoA as cosubstrate)
CC         {ECO:0000269|PubMed:11598135};
CC         KM=57.0 uM for malonyl-CoA (with bisdemalonylsalvianin as
CC         cosubstrate) {ECO:0000269|PubMed:11598135};
CC         KM=14.1 uM for malonyl-CoA (with shisonin as cosubstrate)
CC         {ECO:0000269|PubMed:11598135};
CC       pH dependence:
CC         Optimum pH is 8.0. Active over the pH range 6.0-11.0. Stable at pH
CC         7.5 for 20 hours at 20 degrees Celsius.
CC         {ECO:0000269|PubMed:11598135};
CC       Temperature dependence:
CC         Stable below 30 degrees Celsius for 20 minutes at pH 7.0.
CC         {ECO:0000269|PubMed:11598135};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Detected in petals and sepals, and at lower levels
CC       in bracts and red stems. {ECO:0000269|PubMed:11598135}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels are present in the petals and
CC       sepals of young to opening flowers. {ECO:0000269|PubMed:11598135}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000255}.
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DR   EMBL; AF405707; AAL50566.1; -; mRNA.
DR   AlphaFoldDB; Q8W1W9; -.
DR   SMR; Q8W1W9; -.
DR   KEGG; ag:AAL50566; -.
DR   BRENDA; 2.3.1.172; 7433.
DR   SABIO-RK; Q8W1W9; -.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0033810; F:anthocyanin 5-O-glucoside 6'''-O-malonyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Phenylpropanoid metabolism; Transferase.
FT   CHAIN           1..462
FT                   /note="Malonyl-coenzyme:anthocyanin 5-O-glucoside-6'''-O-
FT                   malonyltransferase"
FT                   /id="PRO_0000405127"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:12578391"
FT   ACT_SITE        390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:12578391"
FT   MUTAGEN         45
FT                   /note="Y->A: Activity reduced to 11% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         150
FT                   /note="Q->A: Activity reduced to 67% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         166
FT                   /note="H->A: Activity reduced to 23% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         167
FT                   /note="H->A: Activity reduced to 0.02% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         168
FT                   /note="C->A: Activity reduced to 8% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         171
FT                   /note="D->A: Activity reduced to 0.8% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         258
FT                   /note="K->A: Activity reduced to 61% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         301
FT                   /note="R->A: Activity reduced to 17% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         315
FT                   /note="N->A: Activity reduced to 1.1% of wild-type."
FT                   /evidence="ECO:0000269|PubMed:12578391"
FT   MUTAGEN         390
FT                   /note="D->A: Activity abolished."
FT                   /evidence="ECO:0000269|PubMed:12578391"
SQ   SEQUENCE   462 AA;  50724 MW;  220B4853BC94DB2F CRC64;
     MTTTTTILET CHIPPPPAAN DLSIPLSFFD IKWLHYHPVR RLLFYHHPSS KSQFLHTIVP
     HLKQSLSLAL THYLPVAGNL LYPSNTEKFP QLRYAAGDSV PVTIAESNSD FESLTGNHTR
     DADQFYDLLP PIPPIEEESD WKLINIFAVQ ITLFPGEGIC IGFSNHHCLG DARSIVGFIS
     AWGEINGIGG YEGFLSNHSD SLSLPIFDRS FINDPNKIDA IFWKVLRNIP LKTASFPLPT
     NRVRSTFLLR RSDIEKLKTA TKSPASSFVA AAAFVWSCMV KSGDKSDENA PELFIIPADA
     RGRVDPPIPE NYFGNCIVSS VAQVERGKLA AEDGFAVAAE AIGGEIEGKL KNRDEILRGA
     ENWMSDIFKC FGMSVLGVSG SPKFDLLKAD FGWGKARKLE VLSIDGENHS MSLCSSSDFN
     GGLEVGLSLP RERMAAFEEV FRASIMAASG PARRSPALVE PL
 
 
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