HMPTM_METJA
ID HMPTM_METJA Reviewed; 506 AA.
AC Q58036;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=7,8-dihydro-6-hydroxymethylpterin dimethyltransferase {ECO:0000305|PubMed:25002541};
DE Short=6-hydroxymethyl-H(2)pterin dimethyltransferase {ECO:0000305|PubMed:25002541};
DE EC=2.1.1.- {ECO:0000269|PubMed:25002541};
GN OrderedLocusNames=MJ0619;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A METHYLTRANSFERASE, REACTION MECHANISM, AND MUTAGENESIS OF
RP CYS-77 AND CYS-102.
RX PubMed=25002541; DOI=10.1128/jb.01903-14;
RA Allen K.D., Xu H., White R.H.;
RT "Identification of a unique radical S-Adenosylmethionine methylase likely
RT involved in methanopterin biosynthesis in Methanocaldococcus jannaschii.";
RL J. Bacteriol. 196:3315-3323(2014).
CC -!- FUNCTION: Is responsible for the addition of methyl groups at C-7 and
CC C-9 of the pterin ring during methanopterin (MPT) biosynthesis.
CC Catalyzes methylation of 7,8-dihydro-6-hydroxymethylpterin, likely
CC using methylenetetrahydromethanopterin as a methyl group donor, via a
CC radical-based mechanism. {ECO:0000269|PubMed:25002541}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:25002541};
CC Note=Binds 2 [4Fe-4S] clusters. The clusters are coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000305|PubMed:25002541};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000305|PubMed:25002541};
CC Note=Binds 2 S-adenosyl-L-methionine per subunit.
CC {ECO:0000305|PubMed:25002541};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000303|PubMed:25002541}.
CC -!- MISCELLANEOUS: The most N-terminal iron-sulfur cluster is involved in
CC C-9 methylation, while the second cluster is required for C-7
CC methylation of the pterin ring. Moreover, C-7 methylation occurs before
CC C-9 methylation. {ECO:0000269|PubMed:25002541}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB98614.1; -; Genomic_DNA.
DR PIR; C64377; C64377.
DR RefSeq; WP_010870124.1; NC_000909.1.
DR AlphaFoldDB; Q58036; -.
DR SMR; Q58036; -.
DR STRING; 243232.MJ_0619; -.
DR DNASU; 1451485; -.
DR EnsemblBacteria; AAB98614; AAB98614; MJ_0619.
DR GeneID; 1451485; -.
DR KEGG; mja:MJ_0619; -.
DR eggNOG; arCOG00933; Archaea.
DR HOGENOM; CLU_023791_0_0_2; -.
DR InParanoid; Q58036; -.
DR OMA; RCDIHYA; -.
DR OrthoDB; 13164at2157; -.
DR PhylomeDB; Q58036; -.
DR BioCyc; MetaCyc:MON-18796; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR034471; 7_8-dihydro-6-hydroxymethylpte.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034474; Methyltransferase_Class_D.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43306; PTHR43306; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00385; 7_8-dihydro-6-hydroxymethylpte; 1.
DR SFLD; SFLDG01100; methyltransferase_(Class_D); 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..506
FT /note="7,8-dihydro-6-hydroxymethylpterin
FT dimethyltransferase"
FT /id="PRO_0000106960"
FT DOMAIN 82..300
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000303|PubMed:25002541"
FT MUTAGEN 77
FT /note="C->A: Loss of C9-methylation but C7-methylation is
FT still observed."
FT /evidence="ECO:0000269|PubMed:25002541"
FT MUTAGEN 102
FT /note="C->A: Loss of methylation activity."
FT /evidence="ECO:0000269|PubMed:25002541"
SQ SEQUENCE 506 AA; 57482 MW; 25FA1F6A380398D8 CRC64;
MEKKTLSLCP ICLKRIPATI LEEDGKIIIK KTCPEHGEFK DIYWGDAELY KKFDKYEFIG
KIEVTNTKVK NGCPYDCGLC PNHKSTTILA NIDVTNRCNL NCPICFANAN KSGKVYEPSF
EDIKRMMENL RKEIPPTPAI QFAGGEPTVR SDLPELIKLA RDMGFLHVQL ATNGIKLKNI
NYLKKLKEAG LSTIYLQFDG ISEKPYLVAR GKNLLPIKQK VIENCKKVGF DSVVLVPTLV
RGVNDNEVGG IIRYAAENVD VVRGINFQPV SFTGRVDEKT LLEGRITIPD FIKLVEEQTD
GEITEEDFYP VPSVAPISVL VEKLTNDRKP TLSSHQHCGT STYVFVDEDG KLIPITRFID
VEGFLEIVKE KIEEIGKSKM HDVKVLGEIA LKLPSLIDLD KAPKSVNIKK IIDLILSVLK
SDYSALAELH YHMLMISCMH FMDAYNFDVK RVMRCCIHYA TPDDRIIPFC TYNTLHRQEV
EEKFSIPLEE WKRMHKIGGE DDREDY
