TAM_AZOSB
ID TAM_AZOSB Reviewed; 253 AA.
AC A1K8U5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=azo2633;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM406670; CAL95250.1; -; Genomic_DNA.
DR RefSeq; WP_011766360.1; NC_008702.1.
DR AlphaFoldDB; A1K8U5; -.
DR SMR; A1K8U5; -.
DR STRING; 62928.azo2633; -.
DR EnsemblBacteria; CAL95250; CAL95250; azo2633.
DR KEGG; azo:azo2633; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_4; -.
DR OMA; YLAFADH; -.
DR OrthoDB; 1739932at2; -.
DR Proteomes; UP000002588; 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 Gene3D; 1.10.150.290; -; 1.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..253
FT /note="Trans-aconitate 2-methyltransferase"
FT /id="PRO_1000056554"
SQ SEQUENCE 253 AA; 28297 MW; D87A0196D3BA605C CRC64;
MPTWDDQQYL KFADERTRAA RDLLARVPLD DAATVVDLGC GPGNSTALLV ERWPQARVVG
VDSSAEMLRS ARQALPQVEW MQADLRAWAP AAPVDLIFAN AVMQWLPDHA TLLPELLRHL
RPGGVLAIQM PRNYDEPSHR LMRETPGPWA ARLAGARAIA PLPAAAWYYD LLAPHARQLE
LWQTTYEQVM DDAGAIVEWV RGTGLRPYLE ALAEDEHPAY LAAYEAGIDA AYPPRSDGRR
LFPFPRLFMV AVR