ID A0A0X3BLV1_9EURY Unreviewed; 523 AA.
AC A0A0X3BLV1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CVK33102.1};
GN ORFNames=MMAB1_1889 {ECO:0000313|EMBL:CVK33102.1};
OS Methanoculleus bourgensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=83986 {ECO:0000313|EMBL:CVK33102.1, ECO:0000313|Proteomes:UP000069850};
RN [1] {ECO:0000313|EMBL:CVK33102.1, ECO:0000313|Proteomes:UP000069850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Methanoculleus sp MAB1 {ECO:0000313|EMBL:CVK33102.1};
RA Manzoor S.;
RL Submitted (JAN-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT158599; CVK33102.1; -; Genomic_DNA.
DR RefSeq; WP_062263842.1; NZ_LT158599.1.
DR AlphaFoldDB; A0A0X3BLV1; -.
DR GeneID; 27137646; -.
DR KEGG; mema:MMAB1_1889; -.
DR OrthoDB; 49957at2157; -.
DR Proteomes; UP000069850; Chromosome chrI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.630.30; -; 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; 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; 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; 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 Iron {ECO:0000256|PIRSR:PIRSR005669-1};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR005669-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR005669-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069850};
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 68..343
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 366..523
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 83
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 88
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 91
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 523 AA; 58403 MW; 4223671B3A92200C CRC64;
MNDTGILREI ISRIFSTGSD PDIQRIKLAV CREYSTNMPK NSAILAAATP EERERLRPLL
LVKPTRTLSG VAPVAVMTSP HPCPHGKCLP CPGGPEHPFA SPQSYTGEEP AALRAREHAF
DPYDQVQARL GQFEALGHHV DKTELIVMGG TMTARPLEYQ EWFVGAAVQA MNDYPGAGVP
AAKPDLDAIF AANESSGVRC VAITFETRPD WCREEHINRM LGMGVTKVEL GVQHLDDRIL
DYNRRGHGVA ESVEANCLLR DAGLKVGFHM MPNLPGASME DDRWMFRELF ADSRFRPDFL
KIYPTLVTPG SEIEALWERG DYRPYSEDEL IDLIAYGKSL LPEYVRLQRI QRDIPAKLIV
AGSRHSNFRQ LAGERLCEQG LRCRCIRCRE VGRTPAPEEV AVSTYAYASC GGEERFIQAG
SEDALVGFAR LRFPHRTFRE ELSGAALLRE LHVYGSVVPL STPAEGDEWQ HRSFGARLLS
RAEEEARDQG FARVAVMSGV GVRPYYRKQG YERVGPYMIK TVV
//
