ID V6JXV6_STRNV Unreviewed; 282 AA.
AC V6JXV6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=M877_25050 {ECO:0000313|EMBL:EST24558.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST24558.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST24558.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST24558.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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:EST24558.1}.
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DR EMBL; AWQW01000172; EST24558.1; -; Genomic_DNA.
DR RefSeq; WP_023541173.1; NZ_CM002280.1.
DR AlphaFoldDB; V6JXV6; -.
DR STRING; 193462.BBN63_20920; -.
DR PATRIC; fig|1352941.4.peg.5100; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_11; -.
DR OrthoDB; 9795085at2; -.
DR Proteomes; UP000017971; 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:0009058; P:biosynthetic process; IEA:UniProt.
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 51..147
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 282 AA; 31115 MW; 6772BFB8D1E90CA5 CRC64;
MRSTTTSPPS TPAPTWDPQQ YLRHSAHRAR PFLDLLARIP ELPNGDRPAR IADIGCGPGN
VTALLAERWP TAHITGYDLS PEMLARAEKE YAGPTPGGGL LDFRLADAAK WTPEEPYDLI
VSNAALQWVP GHAESFAGWT DALTPGGTFA FQVPGNFTAP SHALLGELCE TPRWRERLDS
HGRRFVHILD PADYLVRLTD LGCATDAWET TYLQLLTGED PVLDWVKGTA LRPVLTELAD
DPEEAAQFLV QYGDMLRKAY PPGPHGTVFP FRRIFAVARR QA
//
