ELP3_METJA
ID ELP3_METJA Reviewed; 541 AA.
AC Q58536;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE AltName: Full=Elongator complex protein 3 homolog {ECO:0000305};
GN OrderedLocusNames=MJ1136;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: tRNA uridine(34) acetyltransferase, which mediates formation
CC of carboxymethyluridine in the wobble base at position 34 in tRNAs. The
CC proposed mechanism is the following: (i) recruits S-adenosyl-L-
CC methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-
CC dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii)
CC hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an
CC acetyl radical is formed by the products of the two domains and (iv) is
CC transferred onto the C5 position of uridine(34) in the bound tRNA
CC molecule. Does not show protein lysine acetyltransferase activity.
CC {ECO:0000250|UniProtKB:D5VRB9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC tRNA = 5'-deoxyadenosine + carboxymethyluridine(34) in tRNA + CoA + 2
CC H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407,
CC Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q02908};
CC -!- PATHWAY: tRNA modification. {ECO:0000250|UniProtKB:D5VRB9}.
CC -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}.
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DR EMBL; L77117; AAB99138.1; -; Genomic_DNA.
DR PIR; G64441; G64441.
DR AlphaFoldDB; Q58536; -.
DR SMR; Q58536; -.
DR STRING; 243232.MJ_1136; -.
DR DNASU; 1452032; -.
DR EnsemblBacteria; AAB99138; AAB99138; MJ_1136.
DR KEGG; mja:MJ_1136; -.
DR eggNOG; arCOG01361; Archaea.
DR HOGENOM; CLU_025983_2_1_2; -.
DR InParanoid; Q58536; -.
DR OMA; TFETRPD; -.
DR PhylomeDB; Q58536; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR034687; ELP3-like.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF0; PTHR11135:SF0; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF16199; Radical_SAM_C; 1.
DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR SFLD; SFLDF00344; ELP3-like; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01211; ELP3; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Acyltransferase; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..541
FT /note="tRNA uridine(34) acetyltransferase"
FT /id="PRO_0000107183"
FT DOMAIN 79..350
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 401..541
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 76..336
FT /note="Radical S-adenosyl-L-methionine (rSAM)"
FT /evidence="ECO:0000250|UniProtKB:D5VRB9"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 156
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 467..470
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 491..493
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 524
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
SQ SEQUENCE 541 AA; 62443 MW; 31794B06F11E0BFD CRC64;
MVIIMDEKAK LMRCIIERIL DEYNKGKTLD KKRIEQIKAE CLRIHRIGIG HPSNSEILQY
ATEEEKKILI PILRKKPVRT ISGVAVVAVM TSPEKCPHGK CIFCPGGVGS VFGDVPQSYT
GREPATMRGL MFNFDPYLQT KARIEQLEKV GHPTNKIELI IMGGTFPARD IEYQDWFIKR
CLDAMNGVDA SSLEEAQKIN ETAEHRCVAL CIETRPDYCG EKEINQMLKL GATRVELGVQ
TIYNEILEFC KRGHTVEDTI KATQLLKDSG LKVSYHLMPG MPGSDMEMDK KMFKEIFENP
DFKPDMVKIY PCLVIEGTEL YEMWKRGEYK PYREEEAIEI ISYAKSIMPK WVRTSRIQRD
IPATVIVDGV KKSNLGELVY KYMEKHGIKC KCIRCREVGH VMYKKGIMPD IEHIKLCREE
YEASGGTEIF LSYEDVKNDI LIAFLRLREP YKPFRKEIDD NTMLVRQLHV CGQEKPLTKD
LKEITWQHKG YGRKLLEEAE RIAKEEFGKK KILVTSGIGV REYYRKLGYE RVGAYMGKYL
E
