(data stored in SCRATCH9089 zone)

SWISSPROT: CMOB_PASMU

ID   CMOB_PASMU              Reviewed;         321 AA.
AC   Q9CNT5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 102.
DE   RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_01590};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01590};
GN   Name=cmoB {ECO:0000255|HAMAP-Rule:MF_01590}; OrderedLocusNames=PM0340;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-
CC       methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-
CC       carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine
CC         = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:52848, Rhea:RHEA-COMP:13381, Rhea:RHEA-
CC         COMP:13383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:134278,
CC         ChEBI:CHEBI:136877, ChEBI:CHEBI:136879; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01590};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01590}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. CmoB family. {ECO:0000255|HAMAP-Rule:MF_01590}.
DR   EMBL; AE004439; AAK02424.1; -; Genomic_DNA.
DR   RefSeq; WP_010906598.1; NC_002663.1.
DR   SMR; Q9CNT5; -.
DR   EnsemblBacteria; AAK02424; AAK02424; PM0340.
DR   KEGG; pmu:PM0340; -.
DR   PATRIC; fig|272843.6.peg.353; -.
DR   eggNOG; ENOG4105PFA; Bacteria.
DR   eggNOG; COG0500; LUCA.
DR   HOGENOM; HOG000218456; -.
DR   KO; K15257; -.
DR   OMA; CEWRSDF; -.
DR   BioCyc; PMUL272843:G1FZ8-358-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   HAMAP; MF_01590; tRNA_carboxymethyltr_CmoB; 1.
DR   InterPro; IPR010017; CmoB.
DR   InterPro; IPR027555; Mo5U34_MeTrfas-like.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF08003; Methyltransf_9; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00452; TIGR00452; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CNT5.
DR   SWISS-2DPAGE; Q9CNT5.
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..321
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_0000313938"
FT   REGION          151..153
FT                   /note="Carboxy-S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   REGION          180..181
FT                   /note="Carboxy-S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         90
FT                   /note="Carboxy-S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         104
FT                   /note="Carboxy-S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         109
FT                   /note="Carboxy-S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         129
FT                   /note="Carboxy-S-adenosyl-L-methionine; via carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         195
FT                   /note="Carboxy-S-adenosyl-L-methionine; via carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         199
FT                   /note="Carboxy-S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         314
FT                   /note="Carboxy-S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   321 AA;  36747 MW;  9042DA00840600C8 CRC64;
     MIDFRPFYQH IATTHLSAWL ETLPLQLKQW EKQTHGDYAK WAKIVDFLPH LDADHIDLKS
     AVKSESVSPL SAGEQQRLVY HLKQLMPWRK GPYHLHGIHI DCEWRSDFKW DRVLPHLAPL
     KDRTILDVGC GSGYHMWRMV GEGAKIVVGI DPTELFLCQF EAVRKLLNND RRANLIPLGI
     EQMQPLAAFD TVFSMGVLYH RKSPLDHLSQ LKNQLVRGGE LVLETLVVDG DINTVLVPAD
     RYAKMKNVYF IPSVPALINW LEKVGFKNVR CVDVAPTSLA EQRKTDWLEN ESLIDFLDPC
     DHTKTIEGYQ APTRAVILAN K
//

If you have problems or comments...

PBIL Back to PBIL home page