(data stored in ACNUC7421 zone)

SWISSPROT: CMOB_HISS2

ID   CMOB_HISS2              Reviewed;         321 AA.
AC   B0UVK6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 68.
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=HSM_0145;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA31196.1; -; Genomic_DNA.
DR   RefSeq; WP_012340593.1; NC_010519.1.
DR   SMR; B0UVK6; -.
DR   EnsemblBacteria; ACA31196; ACA31196; HSM_0145.
DR   GeneID; 31486423; -.
DR   KEGG; hsm:HSM_0145; -.
DR   HOGENOM; HOG000218456; -.
DR   KO; K15257; -.
DR   OMA; CEWRSDF; -.
DR   OrthoDB; 1515497at2; -.
DR   BioCyc; HSOM228400:G1GB8-150-MONOMER; -.
DR   Proteomes; UP000008543; 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; B0UVK6.
DR   SWISS-2DPAGE; B0UVK6.
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..321
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_1000087968"
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;  37151 MW;  84B63E7B408DFC02 CRC64;
     MFDFRPFYQQ IATSTLSAWL ETLPLQLKQW EKQTHGDYIK WSKIIDFLPH LTADHIDLKS
     AVKAETKTPL SSGERQRIIH HLKQLMPWRK GPYHLYGIHI DCEWRSDFKW ERVLPHLAPL
     QNRLVLDVGC GSGYHMWRMV GEGAKMVVGI DPTELFLCQF EAVRKLLNND RRANLIPLGI
     EEMQPLAAFD TVFSMGVLYH RKSPLDHLTQ LKNQLVKDGE LVLETLVVEG DINTILVPTD
     RYAKMKNVYF IPSVLALINW LEKCGFHNIR CVDVETTGLE EQRKTDWLEN ESLIDFLNPQ
     DHSKTIEGYP APKRAVILAN K
//

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