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Database: UniProt
Entry: A0A1I7KCE3_9BURK
LinkDB: A0A1I7KCE3_9BURK
Original site: A0A1I7KCE3_9BURK 
ID   A0A1I7KCE3_9BURK        Unreviewed;       261 AA.
AC   A0A1I7KCE3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00560, ECO:0000256|SAAS:SAAS00014025};
DE            EC=2.1.1.144 {ECO:0000256|HAMAP-Rule:MF_00560, ECO:0000256|SAAS:SAAS00014025};
GN   Name=tam {ECO:0000256|HAMAP-Rule:MF_00560};
GN   ORFNames=SAMN05216350_109123 {ECO:0000313|EMBL:SFU95108.1};
OS   Polaromonas sp. YR568.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFU95108.1, ECO:0000313|Proteomes:UP000217451};
RN   [1] {ECO:0000313|EMBL:SFU95108.1, ECO:0000313|Proteomes:UP000217451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR568 {ECO:0000313|EMBL:SFU95108.1,
RC   ECO:0000313|Proteomes:UP000217451};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl
CC       esterification of trans-aconitate. {ECO:0000256|HAMAP-
CC       Rule:MF_00560, ECO:0000256|SAAS:SAAS00539528}.
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         ECO:0000256|SAAS:SAAS01118066};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00560,
CC       ECO:0000256|SAAS:SAAS00343259}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam
CC       family. {ECO:0000256|HAMAP-Rule:MF_00560,
CC       ECO:0000256|SAAS:SAAS00539530}.
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DR   EMBL; FPBM01000009; SFU95108.1; -; Genomic_DNA.
DR   Proteomes; UP000217451; 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   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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000217451};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00560,
KW   ECO:0000256|SAAS:SAAS00014019};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00560,
KW   ECO:0000256|SAAS:SAAS00421821, ECO:0000313|EMBL:SFU95108.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00560,
KW   ECO:0000256|SAAS:SAAS00012141};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00560,
KW   ECO:0000256|SAAS:SAAS00012153, ECO:0000313|EMBL:SFU95108.1}.
SQ   SEQUENCE   261 AA;  29074 MW;  6691A73CA25E171E CRC64;
     MSDWNPALYS RYEDERTRPA QELLARVPLV TAARVFDLGC GPGNSTELLA RRFPEAAVTG
     TDNSEAMLVS ARKRLPVAAF ELSDIASWQP GAGDAAPQLI YANAALQWVP DHAALIPRLF
     AALAPGGVLA VQMPDNRDEP THRLMRELAS EAPWKDAIGD YSRLRTELFS IDRYYDLLAD
     KAAHVDVWRT AYQHPMASAA AIVEWVRATG LKPFVDRLPP ELQASYLAEY ERRVARAYPV
     RTDGKLLLAF PRMFIVAQRK S
//
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