TAM_AGRFC
ID TAM_AGRFC Reviewed; 256 AA.
AC Q8UH15;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Atu0870;
GN ORFNames=AGR_C_1589;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK86677.1; -; Genomic_DNA.
DR PIR; AF2683; AF2683.
DR PIR; D97465; D97465.
DR RefSeq; NP_353892.1; NC_003062.2.
DR RefSeq; WP_006312207.1; NC_003062.2.
DR PDB; 2P35; X-ray; 1.95 A; A/B=1-256.
DR PDBsum; 2P35; -.
DR AlphaFoldDB; Q8UH15; -.
DR SMR; Q8UH15; -.
DR STRING; 176299.Atu0870; -.
DR PRIDE; Q8UH15; -.
DR EnsemblBacteria; AAK86677; AAK86677; Atu0870.
DR KEGG; atu:Atu0870; -.
DR PATRIC; fig|176299.10.peg.868; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_5; -.
DR OMA; RFDARYY; -.
DR PhylomeDB; Q8UH15; -.
DR BioCyc; AGRO:ATU0870-MON; -.
DR EvolutionaryTrace; Q8UH15; -.
DR Proteomes; UP000000813; Chromosome circular.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..256
FT /note="Trans-aconitate 2-methyltransferase"
FT /id="PRO_0000218076"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2P35"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2P35"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 178..193
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2P35"
FT TURN 203..208
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2P35"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:2P35"
FT STRAND 242..255
FT /evidence="ECO:0007829|PDB:2P35"
SQ SEQUENCE 256 AA; 28437 MW; 4F35AA046D0596B4 CRC64;
MAWSAQQYLK FEDERTRPAR DLLAQVPLER VLNGYDLGCG PGNSTELLTD RYGVNVITGI
DSDDDMLEKA ADRLPNTNFG KADLATWKPA QKADLLYANA VFQWVPDHLA VLSQLMDQLE
SGGVLAVQMP DNLQEPTHIA MHETADGGPW KDAFSGGGLR RKPLPPPSDY FNALSPKSSR
VDVWHTVYNH PMKDADSIVE WVKGTGLRPY LAAAGEENRE AFLADYTRRI AAAYPPMADG
RLLLRFPRLF VVAVKK
