DMRX_METMA
ID DMRX_METMA Reviewed; 239 AA.
AC Q8PVV3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=MM_1854;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, 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. {ECO:0000303|PubMed:23995635};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q57661}.
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DR EMBL; AE008384; AAM31550.1; -; Genomic_DNA.
DR RefSeq; WP_011033789.1; NC_003901.1.
DR AlphaFoldDB; Q8PVV3; -.
DR SMR; Q8PVV3; -.
DR STRING; 192952.MM_1854; -.
DR EnsemblBacteria; AAM31550; AAM31550; MM_1854.
DR GeneID; 44088515; -.
DR GeneID; 66136669; -.
DR KEGG; mma:MM_1854; -.
DR PATRIC; fig|192952.21.peg.2137; -.
DR eggNOG; arCOG01705; Archaea.
DR HOGENOM; CLU_098523_0_0_2; -.
DR OMA; IVWCITG; -.
DR BioCyc; MetaCyc:MON-18689; -.
DR BRENDA; 1.5.99.15; 3270.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000595; Chromosome.
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: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:1901285; P:5,6,7,8-tetrahydromethanopterin biosynthetic process; IDA:UniProtKB.
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; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR02700; flavo_MJ0208; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
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..239
FT /note="Dihydromethanopterin reductase (acceptor)"
FT /id="PRO_0000430941"
FT DOMAIN 144..175
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 176..205
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
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="2"
FT /evidence="ECO:0000250"
FT BINDING 185
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 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 26491 MW; 4EABDB9FB9E6EACB CRC64;
MSFQRIAWGI TGAGHFLDRS YQVFKELKLR NPELSVNTYV SRAAEEVLRM YGLEQKLVKI
SGGDYLEEIF RESEQGSSSP KVGRFALDRY DALFVTPATS NTVSKIAYGI ADSLVTNAVS
QAVKGRVPVF VVPVDIEGSI ISEMPYNIDR KQCKHCETCP PRENCPHEAI SEKNGVTDQI
DLLKCKGCGI CKELCPYNAI KGGPVEVLVR DVDMRNVEIV KSLQGITVLE SPEAILELF
