ID A0A1A1YA91_9MYCO Unreviewed; 262 AA.
AC A0A1A1YA91;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=A5724_27800 {ECO:0000313|EMBL:OBF28231.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF28231.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) 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:OBF28231.1}.
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DR EMBL; LZHZ01000063; OBF28231.1; -; Genomic_DNA.
DR RefSeq; WP_067809025.1; NZ_LZHZ01000063.1.
DR AlphaFoldDB; A0A1A1YA91; -.
DR STRING; 1834117.A5724_27800; -.
DR OrthoDB; 9795085at2; -.
DR Proteomes; UP000092025; 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; 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; PF13489; Methyltransf_23; 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|HAMAP-Rule:MF_00560,
KW ECO:0000313|EMBL:OBF28231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00560}.
SQ SEQUENCE 262 AA; 29648 MW; 6A2C8AC3F0218A98 CRC64;
MWNPDVYLAF ADHRGRPYYD LLSRVNIDKP RRVVDLGCGP GNLTATLTQR WPSAAIEAWD
SSPEMVDAAR QRGVDAHVGD VREWTPKSDT DVVVTNATLQ WIPDHVELLV RWAGQLPQRA
WIAMQVPGNF DAPSHRAVRE LARREKWSEP LRDFPFREGQ VEDPEGYAAL LSDAGCTVDA
WETTYIHPLS GQNPVLDWIT GTALTPVKSR LDEEQWQDFR RELIPLLDES YPARADGTTF
FPFRRIFVVA QVGSPSRAAS AR
//
