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Database: UniProt
Entry: K2EA35_9BACT
LinkDB: K2EA35_9BACT
Original site: K2EA35_9BACT 
ID   K2EA35_9BACT            Unreviewed;       561 AA.
AC   K2EA35;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN   ORFNames=ACD_18C00229G0005 {ECO:0000313|EMBL:EKE06953.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE06953.1};
RN   [1] {ECO:0000313|EMBL:EKE06953.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC         tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA
CC         + 2 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:0000256|ARBA:ARBA00034985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC         Evidence={ECO:0000256|ARBA:ARBA00034985};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: tRNA modification. {ECO:0000256|ARBA:ARBA00005217}.
CC   -!- SIMILARITY: Belongs to the ELP3 family.
CC       {ECO:0000256|ARBA:ARBA00005494}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKE06953.1}.
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DR   EMBL; AMFJ01006929; EKE06953.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2EA35; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR039661; ELP3.
DR   InterPro; IPR034687; ELP3-like.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR032432; Radical_SAM_C.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   NCBIfam; TIGR01211; ELP3; 1.
DR   PANTHER; PTHR11135:SF2; ELONGATOR COMPLEX PROTEIN 3; 1.
DR   PANTHER; PTHR11135; HISTONE ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF16199; Radical_SAM_C; 1.
DR   SFLD; SFLDF00344; ELP3-like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          73..374
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   561 AA;  64794 MW;  FEA5925079B9344C CRC64;
     MEEELEKILL EIISHHPKTK DDFNDARRRI CGKMKTVQPS NMKLFKAYQN LLKKKSVKAD
     KNLELLLRKA DIRSMSGVAI ITSLIKPYTC PGQCIYCPTE VKMPKSYIAT EPAAARALAL
     AFSPYRQMQM RLEMLEKTGH PTDKIEYILK GGTWNAYPLR YQYWFILESF KACNDLTRKT
     PTKATLEKDW KEKTLEDLQN ALAIEQEYND KKSKHKIIGL TLETRPDAIS PKTIWHMREQ
     GCTRIELGLQ APDDKILELV KRGHTVEQFR QAILLLRQAG FKVDLHFMPD LPGTTAKHDV
     EMYASLFTDE GLKPDMVKIY PCTVIKSAEL YSWFESGKYK PYASQDLFKA ILEMKKLTPY
     YCRISRLIRD IPSNEIEGGN AITNLREALE KELHKQGEYC KCLRCREVGH AEKIHKIKAD
     KLIPQLFVEE FQTRGGREFF LSLEDEKRRV VFAFLRLRLP EYNDKIKKSE ILEKYLGLGD
     LKKLAYVREL HTYGQLVNVG DKNSSASQHK GMGTKLVKEA DKIARENGYT KIAVISGVGV
     RSYYRKFGYK KIGTYMAKNL K
//
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