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Database: UniProt
Entry: R9T707_METII
LinkDB: R9T707_METII
Original site: R9T707_METII 
ID   R9T707_METII            Unreviewed;       258 AA.
AC   R9T707;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase {ECO:0000313|EMBL:AGN25456.1};
GN   ORFNames=MMINT_00400 {ECO:0000313|EMBL:AGN25456.1};
OS   Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC   Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX   NCBI_TaxID=1295009 {ECO:0000313|EMBL:AGN25456.1, ECO:0000313|Proteomes:UP000014070};
RN   [1] {ECO:0000313|EMBL:AGN25456.1, ECO:0000313|Proteomes:UP000014070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Issoire-Mx1 {ECO:0000313|EMBL:AGN25456.1,
RC   ECO:0000313|Proteomes:UP000014070};
RX   PubMed=23846268; DOI=10.1128/genomeA.00453-13;
RA   Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA   Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA   O'Toole P.W., Brugere J.F.;
RT   "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT   Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT   human feces.";
RL   Genome Announc. 1:142-142(2013).
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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DR   EMBL; CP005934; AGN25456.1; -; Genomic_DNA.
DR   RefSeq; WP_020447981.1; NC_021353.1.
DR   AlphaFoldDB; R9T707; -.
DR   STRING; 1295009.MMINT_00400; -.
DR   GeneID; 41322486; -.
DR   KEGG; mer:MMINT_00400; -.
DR   HOGENOM; CLU_070996_0_0_2; -.
DR   InParanoid; R9T707; -.
DR   OrthoDB; 375447at2157; -.
DR   Proteomes; UP000014070; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833:SF2; BIFUNCTIONAL HOMOCYSTEINE S-METHYLTRANSFERASE_5,10-METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AGN25456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014070};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGN25456.1}.
FT   DOMAIN          1..246
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   258 AA;  28221 MW;  6D0AB2205EFB24F3 CRC64;
     MFIISERING QFISVGKAID NRDSKFIQEL ALKQVDSGAQ ALDVNVGPGR DNGPEDMTWL
     VSTVQEVTEV PLCIDAFGPK TMEAGVKACN NPIIMNSTNA DPARMEKYFP ICREYNADII
     CLCMDEKGIP NSADARAEMA MLMMATAMEY EIMPDRLFLD PLVMPVCAAQ DQCAKVIQAV
     SMFQSLNEPA PRTVVGLSNV SNGAKNRSLI NTTYLAMLMG AGLSSAIMDP EDKELMDALK
     AGEILLNRSL YCDDFLRA
//
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