MER_METKA
ID MER_METKA Reviewed; 349 AA.
AC Q8TXY4; Q49598;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=5,10-methylenetetrahydromethanopterin reductase {ECO:0000305};
DE EC=1.5.98.2 {ECO:0000269|PubMed:1953299};
DE AltName: Full=Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase {ECO:0000303|PubMed:8522533};
DE AltName: Full=Methylene-H(4)MPT reductase {ECO:0000305};
GN Name=mer {ECO:0000303|PubMed:8522533}; OrderedLocusNames=MK0524;
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].
RX PubMed=8522533; DOI=10.1128/jb.177.24.7238-7244.1995;
RA Noelling J., Pihl T.D., Reeve J.N.;
RT "Cloning, sequencing, and growth phase-dependent transcription of the
RT coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase-
RT encoding genes from Methanobacterium thermoautotrophicum delta H and
RT Methanopyrus kandleri.";
RL J. Bacteriol. 177:7238-7244(1995).
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 2-27, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=1953299; DOI=10.1007/bf00245355;
RA Ma K., Linder D., Stetter K.O., Thauer R.K.;
RT "Purification and properties of N5,N10-methylenetetrahydromethanopterin
RT reductase (coenzyme F420-dependent) from the extreme thermophile
RT Methanopyrus kandleri.";
RL Arch. Microbiol. 155:593-600(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=10891279; DOI=10.1006/jmbi.2000.3909;
RA Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K.,
RA Ermler U.;
RT "Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin
RT reductase from two methanogenic archaea.";
RL J. Mol. Biol. 300:935-950(2000).
CC -!- FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT to
CC methyl-H(4)MPT. {ECO:0000269|PubMed:1953299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyl-5,6,7,8-tetrahydromethanopterin + H(+) + oxidized
CC coenzyme F420-(gamma-L-Glu)(n) = 5,10-
CC methylenetetrahydromethanopterin + reduced coenzyme F420-(gamma-L-
CC Glu)(n); Xref=Rhea:RHEA:21144, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57818, ChEBI:CHEBI:58116,
CC ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.2;
CC Evidence={ECO:0000269|PubMed:1953299};
CC -!- ACTIVITY REGULATION: Requires the presence of relatively high
CC concentrations of either sulfate or phosphate for maximal activity.
CC {ECO:0000269|PubMed:1953299}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for methylene-H(4)MPT {ECO:0000269|PubMed:1953299};
CC KM=4 uM for reduced coenzyme F420 {ECO:0000269|PubMed:1953299};
CC Vmax=435 umol/min/mg enzyme (at 65 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:1953299};
CC Note=kcat is 275 sec(-1). {ECO:0000269|PubMed:1953299};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl-
CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step
CC 1/2. {ECO:0000269|PubMed:1953299}.
CC -!- SUBUNIT: Homotetramer composed of two loosely associated dimers.
CC {ECO:0000269|PubMed:10891279}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the mer family. {ECO:0000305}.
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DR EMBL; U31567; AAA92085.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01739.1; -; Genomic_DNA.
DR PDB; 1EZW; X-ray; 1.65 A; A=1-349.
DR PDBsum; 1EZW; -.
DR AlphaFoldDB; Q8TXY4; -.
DR SMR; Q8TXY4; -.
DR STRING; 190192.MK0524; -.
DR EnsemblBacteria; AAM01739; AAM01739; MK0524.
DR KEGG; mka:MK0524; -.
DR PATRIC; fig|190192.8.peg.558; -.
DR HOGENOM; CLU_027853_5_3_2; -.
DR OMA; VCWAAEA; -.
DR BRENDA; 1.5.98.2; 3274.
DR SABIO-RK; Q8TXY4; -.
DR UniPathway; UPA00640; UER00697.
DR EvolutionaryTrace; Q8TXY4; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IDA:MENGO.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 Gene3D; 3.20.20.30; -; 1.
DR HAMAP; MF_01091; F420_mer; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR019946; MeH4methanopterin_reductase.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03555; F420_mer; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methanogenesis;
KW One-carbon metabolism; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1953299"
FT CHAIN 2..349
FT /note="5,10-methylenetetrahydromethanopterin reductase"
FT /id="PRO_0000084808"
FT CONFLICT 21
FT /note="H -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="N -> K (in Ref. 1; AAA92085)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="D -> N (in Ref. 1; AAA92085)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="I -> L (in Ref. 1; AAA92085)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 238..254
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1EZW"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:1EZW"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 292..298
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:1EZW"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:1EZW"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1EZW"
SQ SEQUENCE 349 AA; 37501 MW; 12AF28EDF65F26F0 CRC64;
MAEVSFGIEL LPDDKPTKIA HLIKVAEDNG FEYAWICDHY NNYSYMGVLT LAAVITSKIK
LGPGITNPYT RHPLITASNI ATLDWISGGR AIIGMGPGDK ATFDKMGLPF PCKIPIWNPE
AEDEVGPATA IREVKEVIYQ YLEGGPVEYE GKYVKTGTAD VNARSIQGSD IPFYMGAQGP
IMLKTAGEIA DGVLVNASNP KDFEVAVPKI EEGAKEAGRS LDEIDVAAYT CFSIDKDEDK
AIEATKIVVA FIVMGSPDVV LERHGIDTEK AEQIAEAIGK GDFGTAIGLV DEDMIEAFSI
AGDPDTVVDK IEELLKAGVT QVVVGSPIGP DKEKAIELVG QEVIPHFKE
