MER_METBF
ID MER_METBF Reviewed; 328 AA.
AC Q46FV4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=Mbar_A0254;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69238.1; -; Genomic_DNA.
DR RefSeq; WP_011305293.1; NC_007355.1.
DR PDB; 1Z69; X-ray; 2.61 A; A/B/C/D=1-327.
DR PDBsum; 1Z69; -.
DR AlphaFoldDB; Q46FV4; -.
DR SMR; Q46FV4; -.
DR STRING; 269797.Mbar_A0254; -.
DR EnsemblBacteria; AAZ69238; AAZ69238; Mbar_A0254.
DR GeneID; 3624867; -.
DR KEGG; mba:Mbar_A0254; -.
DR eggNOG; arCOG02410; Archaea.
DR HOGENOM; CLU_027853_5_3_2; -.
DR OMA; VCWAAEA; -.
DR OrthoDB; 46136at2157; -.
DR UniPathway; UPA00640; UER00697.
DR EvolutionaryTrace; Q46FV4; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methanogenesis; One-carbon metabolism;
KW Oxidoreductase.
FT CHAIN 1..328
FT /note="5,10-methylenetetrahydromethanopterin reductase"
FT /id="PRO_1000064889"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 180..197
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:1Z69"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:1Z69"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1Z69"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:1Z69"
SQ SEQUENCE 328 AA; 34592 MW; AC4BD2A64B93ADC7 CRC64;
MKFGIEFVPS DPALKIAYYA KLSEQQGFDH VWITDHYNNR DVYSTLTVLA LNTNSIKIGP
GVTNSYTRNP AITASSIASI AEISGGRAVL GLGPGDKATF DAMGIAWKKP LATTKEAIQA
IRDFISGKKV SMDGEMIKFA GAKLAFKAGN IPIYMGAQGP KMLELAGEIA DGVLINASHP
KDFEVAVEQI KKGAEKAGRD PSEVDVTAYA CFSIDKDPVK AVNAAKVVVA FIVAGSPDLV
LERHGIPVEA KSQIGAAIAK GDFGALMGGL VTPQMIEAFS ICGTPDDCMK RIKDLEAIGV
TQIVAGSPIG PAKEKAIKLI GKEIIAKM
