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Protein

tRNA U34 carboxymethyltransferase

Gene

cmoB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. Can also catalyze the SAM-dependent methylation of ho5U, with much lower efficiency.2 Publications

Catalytic activityi

5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-homocysteine.UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei91Carboxy-S-adenosyl-L-methionineUniRule annotationCombined sources1
Binding sitei105Carboxy-S-adenosyl-L-methionineUniRule annotationCombined sources1
Binding sitei110Carboxy-S-adenosyl-L-methionineUniRule annotationCombined sources1
Binding sitei130Carboxy-S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotationCombined sources1
Binding sitei196Carboxy-S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotationCombined sources1
Binding sitei200Carboxy-S-adenosyl-L-methionineUniRule annotationCombined sources1
Binding sitei315Carboxy-S-adenosyl-L-methionineUniRule annotationCombined sources1

GO - Molecular functioni

GO - Biological processi

  • methylation Source: GO_Central
  • protein homotetramerization Source: EcoCyc
  • tRNA wobble uridine modification Source: EcoCyc

Keywordsi

Molecular functionTransferase
Biological processtRNA processing

Enzyme and pathway databases

BioCyciEcoCyc:G7021-MONOMER
MetaCyc:G7021-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA U34 carboxymethyltransferaseUniRule annotationCurated (EC:2.5.1.-UniRule annotation2 Publications)
Gene namesi
Name:cmoB1 PublicationUniRule annotation
Synonyms:yecP
Ordered Locus Names:b1871, JW1860
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14034 cmoB

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91K → A: Decreases affinity toward Cx-SAM and increases affinity toward SAM. Lack of carboxymethyltransferase activity, but can still produce mho5U. 1
Mutagenesisi200Y → A: Slight decrease in Cx-SAM binding affinity. Does not affect carboxymethyltransferase activity. 1
Mutagenesisi315R → A: Slight decrease in Cx-SAM binding affinity. Does not affect carboxymethyltransferase activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001690851 – 323tRNA U34 carboxymethyltransferaseAdd BLAST323

Proteomic databases

PaxDbiP76291
PRIDEiP76291

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260349, 43 interactors
IntActiP76291, 7 interactors
STRINGi316385.ECDH10B_2012

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Helixi17 – 21Combined sources5
Helixi23 – 33Combined sources11
Helixi38 – 48Combined sources11
Beta strandi55 – 62Combined sources8
Beta strandi64 – 66Combined sources3
Helixi73 – 84Combined sources12
Beta strandi94 – 96Combined sources3
Beta strandi99 – 101Combined sources3
Beta strandi104 – 106Combined sources3
Helixi107 – 114Combined sources8
Helixi115 – 117Combined sources3
Beta strandi125 – 129Combined sources5
Helixi135 – 142Combined sources8
Beta strandi146 – 151Combined sources6
Helixi155 – 167Combined sources13
Beta strandi173 – 177Combined sources5
Helixi181 – 183Combined sources3
Beta strandi190 – 197Combined sources8
Helixi199 – 201Combined sources3
Helixi205 – 213Combined sources9
Beta strandi216 – 227Combined sources12
Beta strandi252 – 254Combined sources3
Helixi255 – 264Combined sources10
Beta strandi268 – 277Combined sources10
Turni280 – 282Combined sources3
Helixi294 – 297Combined sources4
Beta strandi302 – 306Combined sources5
Beta strandi309 – 311Combined sources3
Beta strandi314 – 321Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QNUX-ray2.60A/B/C/D/E/F/G/H1-323[»]
4QNVX-ray2.64A/B1-323[»]
4QNXX-ray2.62A/B1-323[»]
ProteinModelPortaliP76291
SMRiP76291
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni152 – 154Carboxy-S-adenosyl-L-methionine bindingUniRule annotationCombined sources3
Regioni181 – 182Carboxy-S-adenosyl-L-methionine bindingUniRule annotationCombined sources2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoB family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105PFA Bacteria
COG0500 LUCA
HOGENOMiHOG000218456
InParanoidiP76291
KOiK15257
OMAiCEWRSDF
PhylomeDBiP76291

Family and domain databases

HAMAPiMF_01590 tRNA_carboxymethyltr_CmoB, 1 hit
InterProiView protein in InterPro
IPR010017 CmoB
IPR027555 mo5U34_MeTrfas-like
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF08003 Methyltransf_9, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
TIGRFAMsiTIGR00452 TIGR00452, 1 hit

Sequencei

Sequence statusi: Complete.

P76291-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDFGNFYSL IAKNHLSHWL ETLPAQIANW QREQQHGLFK QWSNAVEFLP
60 70 80 90 100
EIKPYRLDLL HSVTAESEEP LSAGQIKRIE TLMRNLMPWR KGPFSLYGVN
110 120 130 140 150
IDTEWRSDWK WDRVLPHLSD LTGRTILDVG CGSGYHMWRM IGAGAHLAVG
160 170 180 190 200
IDPTQLFLCQ FEAVRKLLGN DQRAHLLPLG IEQLPALKAF DTVFSMGVLY
210 220 230 240 250
HRRSPLEHLW QLKDQLVNEG ELVLETLVID GDENTVLVPG DRYAQMRNVY
260 270 280 290 300
FIPSALALKN WLKKCGFVDI RIADVSVTTT EEQRRTEWMV TESLADFLDP
310 320
HDPGKTVEGY PAPKRAVLIA RKP
Length:323
Mass (Da):37,007
Last modified:February 1, 1997 - v1
Checksum:i2954B076A83607A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74941.1
AP009048 Genomic DNA Translation: BAA15681.1
PIRiG64949
RefSeqiNP_416385.1, NC_000913.3
WP_000564725.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74941; AAC74941; b1871
BAA15681; BAA15681; BAA15681
GeneIDi946387
KEGGiecj:JW1860
eco:b1871
PATRICifig|1411691.4.peg.377

Similar proteinsi

Entry informationi

Entry nameiCMOB_ECOLI
AccessioniPrimary (citable) accession number: P76291
Secondary accession number(s): O07983
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health