ID L9UEW2_NATMM Unreviewed; 342 AA.
AC L9UEW2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=C500_20441 {ECO:0000313|EMBL:ELY23196.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ELY23196.1, ECO:0000313|Proteomes:UP000011543};
RN [1] {ECO:0000313|EMBL:ELY23196.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543};
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:ELY23196.1}.
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DR EMBL; AOHS01000063; ELY23196.1; -; Genomic_DNA.
DR RefSeq; WP_004217442.1; NZ_AOHS01000063.1.
DR AlphaFoldDB; L9UEW2; -.
DR GeneID; 8824416; -.
DR PATRIC; fig|547559.17.peg.4035; -.
DR OrthoDB; 213164at2157; -.
DR Proteomes; UP000011543; 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:ELY23196.1}.
FT DOMAIN 21..305
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 342 AA; 36203 MW; 0316F53C848C62D0 CRC64;
MNNDTQPGSE PTVGIELTPE HPTERIADLA ALAEDEGFDV AFTSSHYFNR DPFVTLSRMA
EATDTIRLGP GVVNPYESHP VKLAGQAATV DEESNGRAVF GIGAGDRSSL ANLGIEHERP
LRRVLETFGV ARDLWAGDTV SHDGTFAASD ASLNLEPPSG QLPVYVGAQG PHMLRMSAKH
ADGVLVNAAH PKDLEWAAGQ LEHGLEERPD EHGPFEALAF ASVSVADDED DAREAARPPV
AFIVGGAADP VLDRHDIDRE AAEAVSDALS QGNLTEAFGH VTPEMIDAFC IAGTTEQVAE
QFEAVLEFVD GIVVGSPLGP DLEDAVEKAS AAMEQAIAAD ER
//
