ID A0A101FYE0_9CHLR Unreviewed; 541 AA.
AC A0A101FYE0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Elp3/MiaA/NifB-like radical SAM core domain-containing protein {ECO:0000259|SMART:SM00729};
GN ORFNames=XD73_0362 {ECO:0000313|EMBL:KUK46741.1};
OS Anaerolinea thermophila.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46741.1, ECO:0000313|Proteomes:UP000064249};
RN [1] {ECO:0000313|EMBL:KUK46741.1, ECO:0000313|Proteomes:UP000064249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46_16 {ECO:0000313|EMBL:KUK46741.1};
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK46741.1}.
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DR EMBL; LGFU01000009; KUK46741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FYE0; -.
DR PATRIC; fig|167964.4.peg.667; -.
DR Proteomes; UP000064249; Unassembled WGS sequence.
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 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 NCBIfam; TIGR01211; ELP3; 1.
DR PANTHER; PTHR11135:SF0; 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; SFLDG01086; elongater_protein-like; 1.
DR SFLD; SFLDF00344; ELP3-like; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 91..341
FT /note="Elp3/MiaA/NifB-like radical SAM core"
FT /evidence="ECO:0000259|SMART:SM00729"
SQ SEQUENCE 541 AA; 61099 MW; 3E540F5C69DDF268 CRC64;
MKKNKERWQD NKHYSPEELS IARTVLDEIL RGEPVMKAVH SHPLQAGGFI AKHMLVATYH
AMVAEGSLQL DPALLAKIRM KPIRSLSGVT TVTVLTKPHP CPGECIFCPD DEELPKSYLK
LEPGAARAYE NQFDPFLQVS SRLASYDAIG HPTNKIELLI LGGSWTAYPL EYQEWFIKRC
LDAMNGTESQ TLAEAQLTNE SAKQRNVGLV VETRPDTIQP EILAGLRRMG VTKVQIGAQS
FNDHILEINK RGHSHKATLK ACAMLRAAGF KIVMHWMPNL LGASLASDKE DFIKMWADGY
SPDELKIYPT QLVENSQLYQ YWLRGEYKPY TTEELISLIA DLKTTIPEYS RVNRVIRDIP
ASYIKAGNKR SSLRQDVHKE MEKRGTQCRC IRCREIRARS VSEDSLTLVD QCYHPQYAEE
HFLNYTTETD HLAGYLRLSL PEQTTPEAQS IYRQVWSAIP ELEGCAIIRE VHIYGQSLQF
GAEKDGAAQH LGLGSSLIEK AAALSKERGF QKLAVIAAIG TRQYYKERGF NGGNLYMVRE
L
//
