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Database: UniProt
Entry: M0GU49_HALL2
LinkDB: M0GU49_HALL2
Original site: M0GU49_HALL2 
ID   M0GU49_HALL2            Unreviewed;       328 AA.
AC   M0GU49;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=5,10-methylenetetrahydromethanopterin reductase {ECO:0000256|HAMAP-Rule:MF_01091};
DE            EC=1.5.98.2 {ECO:0000256|HAMAP-Rule:MF_01091};
DE   AltName: Full=Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase {ECO:0000256|HAMAP-Rule:MF_01091};
DE   AltName: Full=Methylene-H(4)MPT reductase {ECO:0000256|HAMAP-Rule:MF_01091};
GN   Name=mer {ECO:0000256|HAMAP-Rule:MF_01091};
GN   ORFNames=C456_07477 {ECO:0000313|EMBL:ELZ75083.1};
OS   Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS   (Haloferax alicantei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1230452 {ECO:0000313|EMBL:ELZ75083.1, ECO:0000313|Proteomes:UP000011535};
RN   [1] {ECO:0000313|EMBL:ELZ75083.1, ECO:0000313|Proteomes:UP000011535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa
RC   2.2 {ECO:0000313|Proteomes:UP000011535};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Catalyzes the oxidation of methyl-H(4)MPT to methylene-
CC       H(4)MPT. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01091};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01091}.
CC   -!- SIMILARITY: Belongs to the mer family. {ECO:0000256|HAMAP-
CC       Rule:MF_01091}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ75083.1}.
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DR   EMBL; AOLH01000011; ELZ75083.1; -; Genomic_DNA.
DR   RefSeq; WP_004062963.1; NZ_AOLH01000011.1.
DR   AlphaFoldDB; M0GU49; -.
DR   PATRIC; fig|1230452.3.peg.1423; -.
DR   Proteomes; UP000011535; Unassembled WGS sequence.
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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 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   PANTHER; PTHR43244; -; 1.
DR   PANTHER; PTHR43244:SF1; 5,10-METHYLENETETRAHYDROMETHANOPTERIN REDUCTASE; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01091};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01091};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01091,
KW   ECO:0000313|EMBL:ELZ75083.1}.
FT   DOMAIN          9..293
FT                   /note="Luciferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00296"
SQ   SEQUENCE   328 AA;  34519 MW;  13530D4F64AB9908 CRC64;
     MLGLELTPEH PVDDLVELGA QAEREGYDSC FVSCHYNNRD PFAVLARLAA ETDDIRLGPG
     VANPYELHPV TLAGKVATVA EASGGRGLLG IGPGDPSTLR NLGLEDERGL RSVLEAFKVA
     QKLWDGERVS HDGTFEATDA GLNFDVPGEV PVYVGGEGPH MCRMAGKHAD GLLFNGSHPD
     DLAWAREQVD IGVEDRPDSR GEFTLAAYAS VSVSEDADAA REAARPPVAF IAAGAAPPVL
     DRHGIDADLA GDIGEKISAG DFSEAFDLVT PKMIDAFSMA GTPDDVADRM DAVLEHADGV
     VVGSPVGPDL EEAITLAAAA YRSTSRHR
//
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