(data stored in ACNUC30630 zone)

SWISSPROT: TAM_MYCSJ

ID   TAM_MYCSJ               Reviewed;         254 AA.
AC   A3PTG0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00560};
DE            EC=2.1.1.144 {ECO:0000255|HAMAP-Rule:MF_00560};
GN   Name=tam {ECO:0000255|HAMAP-Rule:MF_00560}; OrderedLocusNames=Mjls_0374;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC       of trans-aconitate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00560};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00560}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC       {ECO:0000255|HAMAP-Rule:MF_00560}.
DR   EMBL; CP000580; ABN96187.1; -; Genomic_DNA.
DR   RefSeq; WP_011557812.1; NC_009077.1.
DR   SMR; A3PTG0; -.
DR   EnsemblBacteria; ABN96187; ABN96187; Mjls_0374.
DR   GeneID; 32422835; -.
DR   KEGG; mjl:Mjls_0374; -.
DR   eggNOG; ENOG4107R6G; Bacteria.
DR   eggNOG; COG4106; LUCA.
DR   HOGENOM; HOG000125295; -.
DR   KO; K00598; -.
DR   OMA; TVFPFRR; -.
DR   BioCyc; MSP164757:G1G8C-379-MONOMER; -.
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   Gene3D; 1.10.150.290; -; 1.
DR   HAMAP; MF_00560; Tran_acon_Me_trans; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR   InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3PTG0.
DR   SWISS-2DPAGE; A3PTG0.
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..254
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_1000056562"
SQ   SEQUENCE   254 AA;  28459 MW;  9525F5BE01E9E505 CRC64;
     MWNPEAYLSF ADHRGRPFFD LLARVGADAP RRVVDLGCGP GNLTVVLRHR WPEAVVEAWD
     NSPEMVAAAR ERGVQANLGD VRGWSPQPDT DVVLSNATLQ WVPEHPELLT RWAGALAAGS
     WLAMQVPGNF DAPSHQAVRR LADREPWAPL LHDIPFRVGK VVETPADYAA LLTDAGCSVD
     AWETTYIHEL TDAHPVLEWI TGTALRPVRS RLTDEQWDRF RAELIPLLDE AYPVRADGRT
     FFPFRRVFVV ARTG
//

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