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Protein

tRNA(Met) cytidine acetyltransferase TmcA

Gene

tmcA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of N(4)-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2).UniRule annotation2 Publications

Catalytic activityi

(Elongator tRNA(Met))-cytidine(34) + ATP + acetyl-CoA + H2O = (elongator tRNA(Met))-N(4)-acetylcytidine(34) + ADP + phosphate + CoA.UniRule annotation2 Publications

Enzyme regulationi

ATP/GTP hydrolysis is stimulated by the addition of acetyl-CoA and tRNA(Met). Binding of acetyl-CoA to TmcA activates both ATPase and tRNA-binding activities.2 Publications

Kineticsi

  1. KM=2.93 µM for ATP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  2. KM=4.16 µM for ATP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication
  3. KM=117 µM for GTP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  4. KM=66.6 µM for GTP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei180 – 1801ATPUniRule annotation1 Publication
    Binding sitei319 – 3191ATPUniRule annotation1 Publication
    Binding sitei499 – 4991Acetyl-CoAUniRule annotation1 Publication
    Binding sitei506 – 5061Acetyl-CoAUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi202 – 21110ATPUniRule annotation1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • tRNA binding Source: EcoCyc
    • tRNA N-acetyltransferase activity Source: EcoCyc

    GO - Biological processi

    • tRNA acetylation Source: EcoCyc
    • tRNA wobble cytosine modification Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7297-MONOMER.
    ECOL316407:JW2459-MONOMER.
    MetaCyc:G7297-MONOMER.
    BRENDAi2.3.1.193. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA(Met) cytidine acetyltransferase TmcAUniRule annotation (EC:2.3.1.193UniRule annotation)
    Gene namesi
    Name:tmcAUniRule annotation
    Synonyms:ypfI
    Ordered Locus Names:b2474, JW2459
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14196. tmcA.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutants lack the ac4C modification, but do not show any growth defects.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi287 – 2871T → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication
    Mutagenesisi291 – 2911Y → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication
    Mutagenesisi292 – 2921E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication
    Mutagenesisi296 – 2961R → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication
    Mutagenesisi301 – 3011K → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication
    Mutagenesisi319 – 3191R → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication
    Mutagenesisi327 – 3271E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication
    Mutagenesisi377 – 3771H → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication
    Mutagenesisi387 – 3871R → A: Abolishes the tRNA-binding capacity, but no loss of activity. 1 Publication
    Mutagenesisi460 – 4601R → A: Loss of tRNA-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 671671tRNA(Met) cytidine acetyltransferase TmcAPRO_0000169239Add
    BLAST

    Proteomic databases

    PaxDbiP76562.
    PRIDEiP76562.

    Interactioni

    Protein-protein interaction databases

    BioGridi4259195. 17 interactions.
    DIPiDIP-12825N.
    IntActiP76562. 8 interactions.
    STRINGi511145.b2474.

    Structurei

    Secondary structure

    1
    671
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1715Combined sources
    Beta strandi21 – 277Combined sources
    Helixi29 – 4214Combined sources
    Beta strandi48 – 503Combined sources
    Turni68 – 703Combined sources
    Beta strandi73 – 797Combined sources
    Helixi86 – 938Combined sources
    Beta strandi101 – 1077Combined sources
    Helixi109 – 1113Combined sources
    Turni112 – 1143Combined sources
    Helixi118 – 1203Combined sources
    Helixi121 – 1244Combined sources
    Helixi133 – 14311Combined sources
    Beta strandi145 – 1539Combined sources
    Helixi178 – 18710Combined sources
    Beta strandi192 – 1998Combined sources
    Helixi205 – 21511Combined sources
    Beta strandi216 – 2183Combined sources
    Beta strandi220 – 2234Combined sources
    Helixi231 – 2377Combined sources
    Helixi238 – 2403Combined sources
    Helixi246 – 2516Combined sources
    Beta strandi257 – 2626Combined sources
    Helixi264 – 2663Combined sources
    Helixi269 – 2768Combined sources
    Beta strandi279 – 29012Combined sources
    Helixi296 – 3049Combined sources
    Beta strandi310 – 3134Combined sources
    Beta strandi318 – 3203Combined sources
    Helixi325 – 3339Combined sources
    Helixi339 – 3424Combined sources
    Beta strandi350 – 3556Combined sources
    Helixi358 – 3614Combined sources
    Helixi364 – 37613Combined sources
    Beta strandi377 – 3804Combined sources
    Helixi382 – 3909Combined sources
    Beta strandi394 – 4007Combined sources
    Beta strandi402 – 41514Combined sources
    Helixi419 – 4268Combined sources
    Helixi436 – 4449Combined sources
    Helixi450 – 4523Combined sources
    Beta strandi453 – 46311Combined sources
    Beta strandi469 – 4713Combined sources
    Helixi472 – 48211Combined sources
    Beta strandi488 – 4958Combined sources
    Helixi498 – 5069Combined sources
    Beta strandi510 – 5145Combined sources
    Turni520 – 5223Combined sources
    Beta strandi526 – 5327Combined sources
    Helixi535 – 55925Combined sources
    Helixi575 – 58612Combined sources
    Turni591 – 5944Combined sources
    Helixi595 – 60410Combined sources
    Helixi610 – 6178Combined sources
    Helixi622 – 6287Combined sources
    Helixi634 – 65017Combined sources
    Helixi654 – 66613Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZPAX-ray2.35A/B1-671[»]
    ProteinModelPortaliP76562.
    SMRiP76562. Positions 1-670.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP76562.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini356 – 531176N-acetyltransferaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni461 – 4633Acetyl-CoA bindingUniRule annotation1 Publication
    Regioni468 – 4747Acetyl-CoA bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily.UniRule annotation
    Contains 1 N-acetyltransferase domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E0I. Bacteria.
    COG1444. LUCA.
    HOGENOMiHOG000283762.
    InParanoidiP76562.
    KOiK06957.
    OMAiCSAHYRT.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    HAMAPiMF_01886. tRNA_acetyltr_TmcA. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    IPR007807. Helicase_dom.
    IPR027417. P-loop_NTPase.
    IPR032672. TmcA/NAT10/Kre33.
    IPR013562. TmcA_N.
    IPR033442. TmcA_tRNA_bind.
    IPR024914. tRNA_acetyltr_TmcA.
    [Graphical view]
    PANTHERiPTHR10925. PTHR10925. 1 hit.
    PfamiPF08351. DUF1726. 1 hit.
    PF13718. GNAT_acetyltr_2. 1 hit.
    PF05127. Helicase_RecD. 1 hit.
    PF17176. tRNA_bind_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF55729. SSF55729. 2 hits.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P76562-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAELTALHTL TAQMKREGIR RLLVLSGEEG WCFEHTLKLR DALPGDWLWI
    60 70 80 90 100
    SPRPDAENHC SPSALQTLLG REFRHAVFDA RHGFDAAAFA ALSGTLKAGS
    110 120 130 140 150
    WLVLLLPVWE EWENQPDADS LRWSDCPDPI ATPHFVQHLK RVLTADNEAI
    160 170 180 190 200
    LWRQNQPFSL AHFTPRTDWY PATGAPQPEQ QQLLKQLMTM PPGVAAVTAA
    210 220 230 240 250
    RGRGKSALAG QLISRIAGRA IVTAPAKAST DVLAQFAGEK FRFIAPDALL
    260 270 280 290 300
    ASDEQADWLV VDEAAAIPAP LLHQLVSRFP RTLLTTTVQG YEGTGRGFLL
    310 320 330 340 350
    KFCARFPHLH RFELQQPIRW AQGCPLEKMV SEALVFDDEN FTHTPQGNIV
    360 370 380 390 400
    ISAFEQTLWQ SDPETPLKVY QLLSGAHYRT SPLDLRRMMD APGQHFLQAA
    410 420 430 440 450
    GENEIAGALW LVDEGGLSQQ LSQAVWAGFR RPRGNLVAQS LAAHGNNPLA
    460 470 480 490 500
    ATLRGRRVSR IAVHPARQRE GTGRQLIAGA LQYTQDLDYL SVSFGYTGEL
    510 520 530 540 550
    WRFWQRCGFV LVRMGNHREA SSGCYTAMAL LPMSDAGKQL AEREHYRLRR
    560 570 580 590 600
    DAQALAQWNG ETLPVDPLND AVLSDDDWLE LAGFAFAHRP LLTSLGCLLR
    610 620 630 640 650
    LLQTSELALP ALRGRLQKNA SDAQLCTTLK LSGRKMLLVR QREEAAQALF
    660 670
    ALNDVRTERL RDRITQWQLF H
    Length:671
    Mass (Da):74,893
    Last modified:February 1, 1997 - v1
    Checksum:i07C5A019570CDA5D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75527.1.
    AP009048 Genomic DNA. Translation: BAA16352.2.
    PIRiA65023.
    RefSeqiNP_416969.1. NC_000913.3.
    WP_000829360.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75527; AAC75527; b2474.
    BAA16352; BAA16352; BAA16352.
    GeneIDi946053.
    KEGGiecj:JW2459.
    eco:b2474.
    PATRICi32120333. VBIEscCol129921_2569.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75527.1.
    AP009048 Genomic DNA. Translation: BAA16352.2.
    PIRiA65023.
    RefSeqiNP_416969.1. NC_000913.3.
    WP_000829360.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZPAX-ray2.35A/B1-671[»]
    ProteinModelPortaliP76562.
    SMRiP76562. Positions 1-670.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259195. 17 interactions.
    DIPiDIP-12825N.
    IntActiP76562. 8 interactions.
    STRINGi511145.b2474.

    Proteomic databases

    PaxDbiP76562.
    PRIDEiP76562.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75527; AAC75527; b2474.
    BAA16352; BAA16352; BAA16352.
    GeneIDi946053.
    KEGGiecj:JW2459.
    eco:b2474.
    PATRICi32120333. VBIEscCol129921_2569.

    Organism-specific databases

    EchoBASEiEB3948.
    EcoGeneiEG14196. tmcA.

    Phylogenomic databases

    eggNOGiENOG4105E0I. Bacteria.
    COG1444. LUCA.
    HOGENOMiHOG000283762.
    InParanoidiP76562.
    KOiK06957.
    OMAiCSAHYRT.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7297-MONOMER.
    ECOL316407:JW2459-MONOMER.
    MetaCyc:G7297-MONOMER.
    BRENDAi2.3.1.193. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP76562.
    PROiP76562.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    HAMAPiMF_01886. tRNA_acetyltr_TmcA. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    IPR007807. Helicase_dom.
    IPR027417. P-loop_NTPase.
    IPR032672. TmcA/NAT10/Kre33.
    IPR013562. TmcA_N.
    IPR033442. TmcA_tRNA_bind.
    IPR024914. tRNA_acetyltr_TmcA.
    [Graphical view]
    PANTHERiPTHR10925. PTHR10925. 1 hit.
    PfamiPF08351. DUF1726. 1 hit.
    PF13718. GNAT_acetyltr_2. 1 hit.
    PF05127. Helicase_RecD. 1 hit.
    PF17176. tRNA_bind_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF55729. SSF55729. 2 hits.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTMCA_ECOLI
    AccessioniPrimary (citable) accession number: P76562
    Secondary accession number(s): P76972
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: September 7, 2016
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA.1 Publication

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.