MER_METTM
ID MER_METTM Reviewed; 321 AA.
AC Q50744; D9PUN5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=5,10-methylenetetrahydromethanopterin reductase {ECO:0000305};
DE EC=1.5.98.2 {ECO:0000269|PubMed:2379499};
DE AltName: Full=Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase {ECO:0000303|PubMed:7649177};
DE AltName: Full=Methylene-H(4)MPT reductase {ECO:0000305};
GN Name=mer {ECO:0000303|PubMed:7649177}; OrderedLocusNames=MTBMA_c03270;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=7649177; DOI=10.1111/j.1432-1033.1995.tb20760.x;
RA Vaupel M., Thauer R.K.;
RT "Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase
RT (Mer) from Methanobacterium thermoautotrophicum strain Marburg -- cloning,
RT sequencing, transcriptional analysis, and functional expression in
RT Escherichia coli of the mer gene.";
RL Eur. J. Biochem. 231:773-778(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP PROTEIN SEQUENCE OF 1-31.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=2379499; DOI=10.1111/j.1432-1033.1990.tb19109.x;
RA Ma K., Thauer R.K.;
RT "Purification and properties of N5, N10-methylenetetrahydromethanopterin
RT reductase from Methanobacterium thermoautotrophicum (strain Marburg).";
RL Eur. J. Biochem. 191:187-193(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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:2379499}.
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:2379499};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for methylene-H(4)MPT {ECO:0000269|PubMed:2379499};
CC KM=3 uM for reduced coenzyme F420 {ECO:0000269|PubMed:2379499};
CC Vmax=6000 umol/min/mg enzyme {ECO:0000269|PubMed:2379499};
CC Note=kcat is 3600 sec(-1). {ECO:0000269|PubMed:2379499};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:2379499};
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:2379499}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2379499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2379499}.
CC -!- SIMILARITY: Belongs to the mer family. {ECO:0000305}.
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DR EMBL; X86477; CAA60203.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL57933.1; -; Genomic_DNA.
DR PIR; S66529; S66529.
DR RefSeq; WP_013295160.1; NC_014408.1.
DR PDB; 1F07; X-ray; 2.00 A; A/B/C/D=1-321.
DR PDBsum; 1F07; -.
DR AlphaFoldDB; Q50744; -.
DR SMR; Q50744; -.
DR STRING; 79929.MTBMA_c03270; -.
DR EnsemblBacteria; ADL57933; ADL57933; MTBMA_c03270.
DR GeneID; 9704033; -.
DR KEGG; mmg:MTBMA_c03270; -.
DR PATRIC; fig|79929.8.peg.321; -.
DR HOGENOM; CLU_027853_5_3_2; -.
DR OMA; VCWAAEA; -.
DR OrthoDB; 46136at2157; -.
DR BRENDA; 1.5.98.2; 7427.
DR UniPathway; UPA00640; UER00697.
DR EvolutionaryTrace; Q50744; -.
DR Proteomes; UP000000345; 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.
FT CHAIN 1..321
FT /note="5,10-methylenetetrahydromethanopterin reductase"
FT /id="PRO_0000084812"
FT CONFLICT 15
FT /note="K -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1F07"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:1F07"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:1F07"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:1F07"
SQ SEQUENCE 321 AA; 33488 MW; 473DB8BD37486D43 CRC64;
MKFGIEFVPN EPIEKIVKLV KLAEDVGFEY AWITDHYNNK NVYETLALIA EGTETIKLGP
GVTNPYVRSP AITASAIATL DELSNGRATL GIGPGDKATF DALGIEWVKP VSTIRDAIAM
MRTLLAGEKT ESGAQLMGVK AVQEKIPIYM GAQGPMMLKT AGEISDGALI NASNPKDFEA
AVPLIKEGAE AAGKSIADID VAAYTCCSID EDAAAAANAA KIVVAFIAAG SPPPVFERHG
LPADTGKKFG ELLGKGDFGG AIGAVDDALM EAFSVVGTPD EFIPKIEALG EMGVTQYVAG
SPIGPDKEKS IKLLGEVIAS F
