Y819_PYRHO
ID Y819_PYRHO Reviewed; 459 AA.
AC O58549;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Uncharacterized methyltransferase PH0819;
DE EC=2.1.1.-;
GN OrderedLocusNames=PH0819;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA29912.1; -; Genomic_DNA.
DR PIR; F71131; F71131.
DR AlphaFoldDB; O58549; -.
DR SMR; O58549; -.
DR STRING; 70601.3257229; -.
DR EnsemblBacteria; BAA29912; BAA29912; BAA29912.
DR KEGG; pho:PH0819; -.
DR eggNOG; arCOG01356; Archaea.
DR OMA; GNWPPAW; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034466; Methyltransferase_Class_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..459
FT /note="Uncharacterized methyltransferase PH0819"
FT /id="PRO_0000184778"
FT DOMAIN 13..145
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT DOMAIN 188..402
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
SQ SEQUENCE 459 AA; 51718 MW; 766BD6444E27C414 CRC64;
MKVMKILLVL PPTESAIKRV VGTTGPPLGL AYLASMVREE HDVKIIDGLA EDLTFSDIAK
IIKKFDPDIV GITATTSAMY DAYTVAKIAK NINENVFVVM GGPHVTFTPE LTMRECPCID
AVVRGEGELT FKELVDALSK GRELKGILGL SYKENGKVRN EPPRPLIQNV DEIPIPSYDL
LPMDKYKADG VPFGVVMTSR GCPFNCVFCS SSLQFGKRWR GHSVERVIEE LSILHYEYGI
KEIEFLDDTF TLNKKRAIDI SLRIKQEGLD ISWTASSRVN TFNEKVAKAM KEGGCHTVYF
GIESASPRIL EFIGKGITPQ QSIDAVKTAK KFGLHALGSF IIGFPDETRE EVEATIKFAK
KLDIDYAQFT IATPYPGTRL WEYAIANNLL LTMNWRKYTT IDPVMKLKHF TSEQISKLLR
KAYISFYLRP KVLIKDIFEH HGFIIKRAIR GLLRVYYQA