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CAMT2_TOBAC
ID   CAMT2_TOBAC             Reviewed;         242 AA.
AC   O24149;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Caffeoyl-CoA O-methyltransferase 2;
DE            EC=2.1.1.104;
DE   AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase 2;
DE            Short=CCoAMT-2;
DE            Short=CCoAOMT-2;
GN   Name=CCOAOMT2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Samsun NN; TISSUE=Leaf;
RX   PubMed=9484483; DOI=10.1023/a:1005969825070;
RA   Martz F., Maury S., Pincon G., Legrand M.;
RT   "cDNA cloning, substrate specificity and expression study of tobacco
RT   caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme.";
RL   Plant Mol. Biol. 36:427-437(1998).
RN   [2]
RP   TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND INDUCTION.
RX   PubMed=10482677; DOI=10.1104/pp.121.1.215;
RA   Maury S., Geoffroy P., Legrand M.;
RT   "Tobacco O-methyltransferases involved in phenylpropanoid metabolism. The
RT   different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-
RT   methyltransferase and caffeic acid/5-hydroxyferulic acid 3/5-O-
RT   methyltransferase classes have distinct substrate specificities and
RT   expression patterns.";
RL   Plant Physiol. 121:215-224(1999).
CC   -!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
CC       hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of
CC       feruloylated polysaccharides. Involved in the reinforcement of the
CC       plant cell wall. Also involved in the responding to wounding or
CC       pathogen challenge by the increased formation of cell wall-bound
CC       ferulic acid polymers. Methylates 5-hydroxyferulolyl-CoA more
CC       efficiently than caffeoyl-CoA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in the bottom and middle parts of
CC       the stems. {ECO:0000269|PubMed:10482677}.
CC   -!- INDUCTION: By wounding and viral infection.
CC       {ECO:0000269|PubMed:10482677}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR   EMBL; U62734; AAC49914.1; -; mRNA.
DR   PIR; T03796; T03796.
DR   RefSeq; XP_016466601.1; XM_016611115.1.
DR   AlphaFoldDB; O24149; -.
DR   SMR; O24149; -.
DR   GeneID; 107789329; -.
DR   KEGG; nta:107789329; -.
DR   OMA; AICAMTV; -.
DR   OrthoDB; 1116724at2759; -.
DR   BRENDA; 2.1.1.104; 3645.
DR   UniPathway; UPA00711; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   2: Evidence at transcript level;
KW   Lignin biosynthesis; Magnesium; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..242
FT                   /note="Caffeoyl-CoA O-methyltransferase 2"
FT                   /id="PRO_0000165698"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         82..83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         158
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         184
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         185
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
SQ   SEQUENCE   242 AA;  27263 MW;  A900B71449010671 CRC64;
     MATNGENGRH QEVGHKSLLQ SDALYQYILE TSVYPREPEP MKELREITAK HPWNLMTTSA
     DEGQFLSMLL KLINAKNTME IGVFTGYSLL ATAMALPDDG KILAMDINRE NYEIGLPIIE
     KAGLAHKIVF REGPALPVLD QMIEDGKYHG SYDFIFVDAD KDNYLNYHKR LIDLVKVGGL
     IGYDNTLWNG SVVAPPDAPL RKYVRYYRDF VLELNKALAA DSRIEICQLP VGDGITLCRR
     IS
 
 
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