DMRX_METJA
ID DMRX_METJA Reviewed; 246 AA.
AC Q57661;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dihydromethanopterin reductase (acceptor) {ECO:0000303|PubMed:23995635};
DE Short=H(2)MPT reductase {ECO:0000303|PubMed:23995635};
DE EC=1.5.99.15 {ECO:0000269|PubMed:23995635};
GN Name=dmrX {ECO:0000303|PubMed:23995635}; OrderedLocusNames=MJ0208;
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, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=23995635; DOI=10.1128/jb.00457-13;
RA Wang S., Tiongson J., Rasche M.E.;
RT "Discovery and characterization of the first archaeal dihydromethanopterin
RT reductase, an iron-sulfur flavoprotein from Methanosarcina mazei.";
RL J. Bacteriol. 196:203-209(2014).
CC -!- FUNCTION: Involved in the biosynthesis of tetrahydromethanopterin, a
CC coenzyme used in methanogenesis. Catalyzes the reduction of
CC dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT).
CC Ferredoxin may serve as an electron donor.
CC {ECO:0000269|PubMed:23995635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + A = 7,8-dihydromethanopterin
CC + AH2; Xref=Rhea:RHEA:42804, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58103, ChEBI:CHEBI:72788; EC=1.5.99.15;
CC Evidence={ECO:0000269|PubMed:23995635};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000303|PubMed:23995635};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000303|PubMed:23995635};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23995635}.
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DR EMBL; L77117; AAB98191.1; -; Genomic_DNA.
DR PIR; A64326; A64326.
DR AlphaFoldDB; Q57661; -.
DR SMR; Q57661; -.
DR STRING; 243232.MJ_0208; -.
DR EnsemblBacteria; AAB98191; AAB98191; MJ_0208.
DR KEGG; mja:MJ_0208; -.
DR eggNOG; arCOG01705; Archaea.
DR HOGENOM; CLU_098523_0_0_2; -.
DR InParanoid; Q57661; -.
DR OMA; IVWCITG; -.
DR PhylomeDB; Q57661; -.
DR BRENDA; 1.5.99.15; 3260.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0044684; F:dihydromethanopterin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IDA:UniProtKB.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IBA:GO_Central.
DR GO; GO:1901285; P:5,6,7,8-tetrahydromethanopterin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR014073; DmrX.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF00037; Fer4; 2.
DR Pfam; PF02441; Flavoprotein; 1.
DR TIGRFAMs; TIGR02700; flavo_MJ0208; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..246
FT /note="Dihydromethanopterin reductase (acceptor)"
FT /id="PRO_0000159308"
FT DOMAIN 150..178
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 179..208
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 27697 MW; 41DAC513C3212721 CRC64;
MNYRFGINMK IVWCITGAGH LLRESFQVMK RLKEEIEDLK VTTLVSRAGE EVVKMYGLFG
ELYNISNGNY YEELILEREH PYSSPITGRL SLGKYDYLIC SPATGNTVAK VVNGIADSLV
TNAIAQAGKG FVKSLIVPVD YKAGIVTTKL PYAIDKKKCK LCLKCINVCP NGAIVKRDNF
VEILLSKCLG CGNCKKVCPY NAIIEGKEIK MRVRKIDAEN TRKLMELEDV IVLKHPYEIL
EFFNIR
