ID I4ERY0_9ACTN Unreviewed; 266 AA.
AC I4ERY0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ECO:0000313|EMBL:CCH86143.1};
GN OrderedLocusNames=MODMU_0686 {ECO:0000313|EMBL:CCH86143.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86143.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH86143.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH86143.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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; FO203431; CCH86143.1; -; Genomic_DNA.
DR RefSeq; WP_014738753.1; NC_017955.1.
DR AlphaFoldDB; I4ERY0; -.
DR STRING; 477641.MODMU_0686; -.
DR KEGG; mmar:MODMU_0686; -.
DR PATRIC; fig|477641.3.peg.656; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_11; -.
DR OMA; YLAFADH; -.
DR OrthoDB; 9795085at2; -.
DR Proteomes; UP000006461; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006461};
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 38..129
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 266 AA; 27685 MW; 0E4FCED6F5D73EC7 CRC64;
MQSPGAWDPT TYLRFAGERA RPFAELVSRV GARAPAVVVD LGCGDGSATA GLAQRWPGAR
VTGVDSSPAM LAAAAAHAVP GRLEFVAGDL RDWRPAGPVD VLVSNAALHW VPGHGDLLAR
WAGDLAPDGW LAVQVPGNQT APTHALLADL VGSRRWRSRL APGGDAVLDP AAVLDPAGYL
DVLSAAGLDA DVWETTYLHV LSGADPVLGW VSGTVLRPVL GRLPPDDADQ LTAEYAAALR
AAYPARADGT TVLPFRRLFA VGHRPG
//
