MTD_METKA
ID MTD_METKA Reviewed; 283 AA.
AC P94951; Q9UWL4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=F420-dependent methylenetetrahydromethanopterin dehydrogenase;
DE Short=MTD;
DE EC=1.5.98.1;
DE AltName: Full=Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase;
GN Name=mtd; OrderedLocusNames=MK0011;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9151968; DOI=10.1111/j.1432-1033.1997.t01-1-00386.x;
RA Klein A.R., Thauer R.K.;
RT "Overexpression of the coenzyme-F420-dependent N5,N10-
RT methylenetetrahydromethanopterin dehydrogenase gene from the
RT hyperthermophilic Methanopyrus kandleri.";
RL Eur. J. Biochem. 245:386-391(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [3]
RP PROTEIN SEQUENCE OF 2-35, AND CHARACTERIZATION.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=8215796; DOI=10.1007/bf00249123;
RA Klein A.R., Koch J., Stetter K.O., Thauer R.K.;
RT "Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme
RT thermophile Methanopyrus kandleri: characterization of the coenzyme F420-
RT dependent enzyme.";
RL Arch. Microbiol. 160:186-192(1993).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=12925803; DOI=10.1107/s0907444903014896;
RA Hagemeier C.H., Shima S., Warkentin E., Thauer R.K., Ermler U.;
RT "Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase
RT from Methanopyrus kandleri: the selenomethionine-labelled and non-labelled
RT enzyme crystallized in two different forms.";
RL Acta Crystallogr. D 59:1653-1655(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
RX PubMed=14499608; DOI=10.1016/s0022-2836(03)00949-5;
RA Hagemeier C.H., Shima S., Thauer R.K., Bourenkov G., Bartunik H.D.,
RA Ermler U.;
RT "Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase
RT (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual
RT quarternary structure.";
RL J. Mol. Biol. 332:1047-1057(2003).
CC -!- FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to
CC methylene-H(4)MPT. {ECO:0000269|PubMed:9151968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methylenetetrahydromethanopterin + 2 H(+) + oxidized
CC coenzyme F420-(gamma-L-Glu)(n) = 5,10-methenyl-5,6,7,8-
CC tetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n);
CC Xref=Rhea:RHEA:16721, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57818, ChEBI:CHEBI:58337,
CC ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.1;
CC -!- ACTIVITY REGULATION: Strictly dependent on the presence of salts for
CC activity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl-5,6,7,8-
CC tetrahydromethanopterin (coenzyme F420 route): step 1/1.
CC -!- SUBUNIT: Homohexamer composed of a trimer of dimers.
CC -!- SIMILARITY: Belongs to the MTD family. {ECO:0000305}.
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DR EMBL; Y10251; CAA71298.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01228.1; -; Genomic_DNA.
DR PDB; 1QV9; X-ray; 1.54 A; A/B/C=1-283.
DR PDB; 1U6I; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-283.
DR PDB; 1U6J; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-283.
DR PDB; 1U6K; X-ray; 1.55 A; A/B/C=1-283.
DR PDB; 3IQE; X-ray; 1.80 A; A/B/C/D/E/F=1-283.
DR PDB; 3IQF; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-283.
DR PDB; 3IQZ; X-ray; 2.10 A; A/B/C/D/E/F=1-283.
DR PDBsum; 1QV9; -.
DR PDBsum; 1U6I; -.
DR PDBsum; 1U6J; -.
DR PDBsum; 1U6K; -.
DR PDBsum; 3IQE; -.
DR PDBsum; 3IQF; -.
DR PDBsum; 3IQZ; -.
DR AlphaFoldDB; P94951; -.
DR SMR; P94951; -.
DR STRING; 190192.MK0011; -.
DR EnsemblBacteria; AAM01228; AAM01228; MK0011.
DR KEGG; mka:MK0011; -.
DR PATRIC; fig|190192.8.peg.10; -.
DR HOGENOM; CLU_1006890_0_0_2; -.
DR OMA; KGCFMTK; -.
DR BRENDA; 1.5.98.1; 3274.
DR UniPathway; UPA00640; UER00695.
DR EvolutionaryTrace; P94951; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0030268; F:methylenetetrahydromethanopterin dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00058; MTD; 1.
DR InterPro; IPR002844; MTD.
DR InterPro; IPR036080; MTD_sf.
DR Pfam; PF01993; MTD; 1.
DR PIRSF; PIRSF005627; MTD; 1.
DR SUPFAM; SSF102324; SSF102324; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Methanogenesis;
KW One-carbon metabolism; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8215796"
FT CHAIN 2..283
FT /note="F420-dependent methylenetetrahydromethanopterin
FT dehydrogenase"
FT /id="PRO_0000075039"
FT REGION 255..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1QV9"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1QV9"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 197..222
FT /evidence="ECO:0007829|PDB:1QV9"
FT HELIX 227..257
FT /evidence="ECO:0007829|PDB:1QV9"
SQ SEQUENCE 283 AA; 31382 MW; D2B778CB34D3034C CRC64;
MTVAKAIFIK CGNLGTSMMM DMLLDERADR EDVEFRVVGT SVKMDPECVE AAVEMALDIA
EDFEPDFIVY GGPNPAAPGP SKAREMLADS EYPAVIIGDA PGLKVKDEME EQGLGYILVK
PDAMLGARRE FLDPVEMAIY NADLMKVLAA TGVFRVVQEA FDELIEKAKE DEISENDLPK
LVIDRNTLLE REEFENPYAM VKAMAALEIA ENVADVSVEG CFVEQDKERY VPIVASAHEM
MRKAAELADE ARELEKSNDA VLRTPHAPDG KVLSKRKFME DPE
