TAM_STRCO
ID TAM_STRCO Reviewed; 303 AA.
AC Q9K3T2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00560};
DE EC=2.1.1.144 {ECO:0000255|HAMAP-Rule:MF_00560};
GN Name=tam {ECO:0000255|HAMAP-Rule:MF_00560}; OrderedLocusNames=SCO3132;
GN ORFNames=SCE66.11c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC of trans-aconitate. {ECO:0000255|HAMAP-Rule:MF_00560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-aconitate = (E)-3-
CC (methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:14969, ChEBI:CHEBI:15708, ChEBI:CHEBI:57470,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.144;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00560};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00560}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC {ECO:0000255|HAMAP-Rule:MF_00560}.
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DR EMBL; AL939115; CAB95925.1; -; Genomic_DNA.
DR RefSeq; NP_627349.1; NC_003888.3.
DR RefSeq; WP_011028784.1; NZ_VNID01000013.1.
DR AlphaFoldDB; Q9K3T2; -.
DR SMR; Q9K3T2; -.
DR STRING; 100226.SCO3132; -.
DR GeneID; 1098566; -.
DR KEGG; sco:SCO3132; -.
DR PATRIC; fig|100226.15.peg.3196; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_11; -.
DR InParanoid; Q9K3T2; -.
DR OMA; YLAFADH; -.
DR PhylomeDB; Q9K3T2; -.
DR BRENDA; 2.1.1.144; 5998.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030798; F:trans-aconitate 2-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.290; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00560; Tran_acon_Me_trans; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..303
FT /note="Trans-aconitate 2-methyltransferase"
FT /id="PRO_0000218087"
FT REGION 271..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 32059 MW; 898290A2422D556A CRC64;
MPATAPTWDP AQYLRHAGHR ARPFTDLLAR IPDLPADPPR IADLGCGPGN VTVLLADRWP
TARITGYDNS PRMLERARQY AGPTSGGGHL DFAPADARSW TPDEPCDLLV SNATLQWVPG
HADLFPGWID RLAPGGTLAL QVPGNFDAPS HRLMRELADS RRWRERLAGV LRHDDAVLTP
EGYLAHLTAA GCTADVWETT YVHLLPGDDA VLDWVRGTGL RPVLDALDGD PAARDAFVDE
YRAVLRAAYP AQAHGTPFPF RRVFAVARKP EGSGGSGGSG GSAGSAGCAG SGGSVGPAGE
AGR