ID   MER_METMA               Reviewed;         328 AA.
AC   Q8PZ66;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=5,10-methylenetetrahydromethanopterin reductase {ECO:0000255|HAMAP-Rule:MF_01091};
DE            EC=1.5.98.2 {ECO:0000255|HAMAP-Rule:MF_01091};
DE   AltName: Full=Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase {ECO:0000255|HAMAP-Rule:MF_01091};
DE   AltName: Full=Methylene-H(4)MPT reductase {ECO:0000255|HAMAP-Rule:MF_01091};
GN   Name=mer {ECO:0000255|HAMAP-Rule:MF_01091}; OrderedLocusNames=MM_0628;
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).
CC   -!- FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT to
CC       methyl-H(4)MPT. {ECO:0000255|HAMAP-Rule:MF_01091}.
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:0000255|HAMAP-Rule:MF_01091};
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:0000255|HAMAP-Rule:MF_01091}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01091}.
CC   -!- SIMILARITY: Belongs to the mer family. {ECO:0000255|HAMAP-
CC       Rule:MF_01091}.
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DR   EMBL; AE008384; AAM30324.1; -; Genomic_DNA.
DR   RefSeq; WP_011032579.1; NC_003901.1.
DR   AlphaFoldDB; Q8PZ66; -.
DR   SMR; Q8PZ66; -.
DR   STRING; 192952.MM_0628; -.
DR   EnsemblBacteria; AAM30324; AAM30324; MM_0628.
DR   GeneID; 44086159; -.
DR   KEGG; mma:MM_0628; -.
DR   PATRIC; fig|192952.21.peg.740; -.
DR   eggNOG; arCOG02410; Archaea.
DR   HOGENOM; CLU_027853_5_3_2; -.
DR   OMA; VCWAAEA; -.
DR   UniPathway; UPA00640; UER00697.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Methanogenesis; One-carbon metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..328
FT                   /note="5,10-methylenetetrahydromethanopterin reductase"
FT                   /id="PRO_0000084809"
SQ   SEQUENCE   328 AA;  34812 MW;  B5120CB00E004542 CRC64;
     MKFGIEFVPA DPALKIAYYA KLSEQQGFDY VWITDHYNNR DVYSTLTVLA LNTNSIKIGS
     GVTNSYTRNP AITASSIASI AEISGGRAVL GLGPGDKATF DAMGIAWEKP LATTKEAIQA
     IRDFIDGKKV SMDGEMVKFA GAKLAFKAGK IPIYMGAQGP KMLELAGEVA DGVLINASHP
     KDFEVAVEQI RKGAEKVGRD PSEVDVTAYA CFSIDKDPVK AVNAAKVVVA FIVAGSPDLV
     LERHGISVEA KKQIGDAIAK GDFGSLMGGL VTPQMIEAFS ICGTPEDCMK RIKDLEAIGV
     TQIVAGSPIG PDKEKAIKLI GKEIIAKM