Y114_METTH
ID Y114_METTH Reviewed; 262 AA.
AC O26217;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Uncharacterized protein MTH_114;
GN OrderedLocusNames=MTH_114;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
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DR EMBL; AE000666; AAB84620.1; -; Genomic_DNA.
DR PIR; G69018; G69018.
DR AlphaFoldDB; O26217; -.
DR SMR; O26217; -.
DR STRING; 187420.MTH_114; -.
DR PRIDE; O26217; -.
DR EnsemblBacteria; AAB84620; AAB84620; MTH_114.
DR KEGG; mth:MTH_114; -.
DR PATRIC; fig|187420.15.peg.85; -.
DR HOGENOM; CLU_009273_10_1_2; -.
DR Proteomes; UP000005223; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024018; CHP04083_rSAM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR PANTHER; PTHR43273; PTHR43273; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR04083; rSAM_pep_methan; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..262
FT /note="Uncharacterized protein MTH_114"
FT /id="PRO_0000134467"
FT DOMAIN 1..211
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ SEQUENCE 262 AA; 30369 MW; D7060C7B82828871 CRC64;
MAFHVMIIPS MNCPSDCSYC WGVDRDSRVM DMETVREMVS WLMEFRNEPA TFTFHGGEPL
LAGYEFYRDT LKLISERLSF LKPAFAIQTN LWLMTDEMAE LFAEYSIPIG SSLDGPREIN
DYQRGDGYFD RTMQGYEIAR KHGLRVSFIS TFTSYSIRRR EEIFNFFLEN GMNLKLHPAL
PSLKSSDPEE WAITAEEYGD LLLYLLDSYL EHFGEIEIQN IDHFAKSAFL RRGLYVHMLI
VWATPSQLTP TVIYTHAIAS LV
