ID A8TT06_9PROT Unreviewed; 255 AA.
AC A8TT06;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00560};
DE EC=2.1.1.144 {ECO:0000256|HAMAP-Rule:MF_00560};
GN Name=tam {ECO:0000256|HAMAP-Rule:MF_00560};
GN ORFNames=BAL199_09273 {ECO:0000313|EMBL:EDP64402.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64402.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP64402.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64402.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC of trans-aconitate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00560};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00560}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC {ECO:0000256|HAMAP-Rule:MF_00560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP64402.1}.
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DR EMBL; ABHC01000009; EDP64402.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TT06; -.
DR STRING; 331869.BAL199_09273; -.
DR eggNOG; COG4106; Bacteria.
DR OrthoDB; 9795085at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.150.290; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR43861:SF1; TRANS-ACONITATE 2-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00560};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00560}; Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00560}.
FT DOMAIN 34..123
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 255 AA; 27776 MW; 02DAD8C194B5D7DE CRC64;
MAWDPAQYLK FADHRLRPAL DLLARIDVAA PGRVIDLGCG TGNVTAILAQ RWPAATVGGI
DDSDTMLARA REEHPGLPFA TANAATWTAS PLVDVLYSNA ALHWLGNHDQ LLPHLFRQVA
PGGWLAVQMP RNFGAPSHTA VADAARDGPW ADRIVPMLAS PPVDEPGVYA SRLAPLADSL
DIWETEYLQI LDGENPVAEW TKGTWLRPFL DALEEPDRSG FEAAYRARVA AAYPPGADGR
TAFPFRRLFL VARRA
//
