ID E6VKX3_RHOPX Unreviewed; 256 AA.
AC E6VKX3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=Rpdx1_1745 {ECO:0000313|EMBL:ADU43362.1};
OS Rhodopseudomonas palustris (strain DX-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43362.1, ECO:0000313|Proteomes:UP000001402};
RN [1] {ECO:0000313|Proteomes:UP000001402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA Woyke T.;
RT "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL Submitted (DEC-2010) 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}.
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DR EMBL; CP002418; ADU43362.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VKX3; -.
DR STRING; 652103.Rpdx1_1745; -.
DR KEGG; rpx:Rpdx1_1745; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_5; -.
DR OrthoDB; 9795085at2; -.
DR BioCyc; RPAL652103:RPDX1_RS08565-MONOMER; -.
DR Proteomes; UP000001402; 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 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}; 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 35..124
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 256 AA; 28717 MW; C69ADE24D6A19A02 CRC64;
MADWNAEQYL KFEDQRTRPA RDLLAQVPTT APRKVADIGC GPGNSTALLV ERWPEAAVIG
VDTSADMLRQ ARERLPHHKF IEANVAHWTA PPGTEVLFAN AVFQWVPDHL KQLKRLLSGL
DDGGVLALQM PDNLDEPSHI LMREVALQER WRHQLSKAAE LRDGLPKPGV YYDALKPLCS
RLEIWHTVYN HALDGPEAIV EWVKGTGLRP FIDPLDLPER KAYLAAYTAR IAAAYPAQGD
GQVLLRFPRI FIVAVK
//
