ID A6UQM2_METVS Unreviewed; 541 AA.
AC A6UQM2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Histone acetyltransferase, ELP3 family {ECO:0000313|EMBL:ABR54794.1};
DE EC=2.3.1.48 {ECO:0000313|EMBL:ABR54794.1};
GN OrderedLocusNames=Mevan_0889 {ECO:0000313|EMBL:ABR54794.1};
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327 {ECO:0000313|EMBL:ABR54794.1, ECO:0000313|Proteomes:UP000001107};
RN [1] {ECO:0000313|EMBL:ABR54794.1, ECO:0000313|Proteomes:UP000001107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB
RC {ECO:0000313|Proteomes:UP000001107};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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|PIRSR:PIRSR005669-1};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|PIRSR:PIRSR005669-1};
CC -!- PATHWAY: tRNA modification. {ECO:0000256|ARBA:ARBA00005217}.
CC -!- SIMILARITY: Belongs to the ELP3 family.
CC {ECO:0000256|ARBA:ARBA00005494}.
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DR EMBL; CP000742; ABR54794.1; -; Genomic_DNA.
DR RefSeq; WP_011972695.1; NC_009634.1.
DR AlphaFoldDB; A6UQM2; -.
DR STRING; 406327.Mevan_0889; -.
DR GeneID; 5326006; -.
DR KEGG; mvn:Mevan_0889; -.
DR eggNOG; arCOG01361; Archaea.
DR HOGENOM; CLU_025983_2_1_2; -.
DR OrthoDB; 49957at2157; -.
DR Proteomes; UP000001107; Chromosome.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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/MiaA/NifB-like_rSAM.
DR InterPro; IPR000182; GNAT_dom.
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; PF13673; Acetyltransf_10; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF16199; Radical_SAM_C; 1.
DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 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.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ABR54794.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR005669-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR005669-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR005669-1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABR54794.1};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 81..350
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 393..541
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
SQ SEQUENCE 541 AA; 61430 MW; 37124D4DC34E3AA8 CRC64;
MSEYSKFIRC IIINLLAEKE KIRGLDPKRK KQKVEDIKAK CLRKHGLNTG FPPNSDVIAH
ATEEEKTEIV PILRKKPIRT LSGVSVVAVM TSPEPCPHGK CSFCPGGKES NFGNVPQSYT
GKEPATMRGI MYDFNPYIQT VERLKQLEKV GHPTDKVELI IMGGTFPARD VGYQESFIKG
CLDAMNGEIS NSLNEAKLKN ESAKHRCVAL TIETRPDYCG EKEINQMLNL GATRVELGIQ
STYGEVLDFV KRGHDIDASI NATRLLKDSG LKVSYHIIPG LPNTTFEMDK KMIETIFEDN
RYKPDLIKFY PCLVIPGTEI YDLWKQGKFS PMNDEKAIEL IVYGKSIMPK WIRTSRIQRD
IPATVINEGV RKSNLGELVY NRLEELGIKC KCIRCREVGH VGYKKGIFPE IENIKLYRTD
YDANFGKEVF LSFEDLKNDL LIGYLRLRIP SKPFRPEITD NTSIIRQVHV CGQQKELDAS
SIESSWQHKG YGRLLIEEAE KISKEEFGKN QILINSGIGV IEYYKKLGYK KVGPYMGKIL
K
//
