ID MTD_ARCFU Reviewed; 273 AA. AC O29544; Q9UWM0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 63. DE RecName: Full=F420-dependent methylenetetrahydromethanopterin dehydrogenase; DE Short=MTD; DE EC=1.5.99.9; DE AltName: Full=Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase; GN Name=mtd; OrderedLocusNames=AF_0714; OS Archaeoglobus fulgidus. OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Archaeoglobus. OX NCBI_TaxID=2234; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126; RX MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., RA Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., RA Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., RA Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., RA Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., RA Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., RA Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., RA Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., RA Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., RA Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., RA Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate- RT reducing archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). RN [2] RP PROTEIN SEQUENCE OF 2-34, AND CHARACTERIZATION. RC STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126; RX MEDLINE=93243884; PubMed=8481089; DOI=10.1007/BF00248476; RA Schworer B., Breitung J., Klein A.R., Stetter K.O., Thauer R.K.; RT "Formylmethanofuran: tetrahydromethanopterin formyltransferase and RT N5,N10-methylenetetrahydromethanopterin dehydrogenase from the RT sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes RT from methanogenic Archaea."; RL Arch. Microbiol. 159:225-232(1993). CC -!- FUNCTION: Catalyzes the oxidation of methylene-H(4)MPT to CC methenyl-H(4)MPT(+). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydromethanopterin + CC coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced CC coenzyme F420. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is about 5.5; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. Thermostable up to 90 CC degrees Celsius, however, only in the presence of salts; CC -!- PATHWAY: Metabolic intermediate metabolism; lactic acid oxidation. CC -!- SIMILARITY: Belongs to the MTD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000782; AAB90526.1; -; Genomic_DNA. DR PIR; B69339; B69339. DR RefSeq; NP_069548.1; -. DR GeneID; 1483932; -. DR GenomeReviews; AE000782_GR; AF_0714. DR KEGG; afu:AF0714; -. DR NMPDR; fig|224325.1.peg.707; -. DR TIGR; AF_0714; -. DR HOGENOM; O29544; -. DR OMA; O29544; NPYAKAK. DR BioCyc; AFUL224325:AF_0714-MON; -. DR BRENDA; 1.5.99.9; 7576. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0030268; F:methylenetetrahydromethanopterin dehydrogen...; IEA:HAMAP. DR GO; GO:0015948; P:methanogenesis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00058; -; 1. DR InterPro; IPR002844; Methylene_DH. DR Pfam; PF01993; MTD; 1. DR PIRSF; PIRSF005627; MTD; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; One-carbon metabolism; KW Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 273 F420-dependent FT methylenetetrahydromethanopterin FT dehydrogenase. FT /FTId=PRO_0000075036. SQ SEQUENCE 273 AA; 29645 MW; 335B2432D5FE7B7E CRC64; MVVKVGVLKM GAIGTALLVE YLLDERADRE DIEVRVVTSG AKMQPEEAVV AEKLKEFDPD VVIVVSPNAA LPGPKAAREA FEGKPVIVIS DAPAKKAKDE LKEKGFGYIL INADSMIGAR REFLDPTEMA LFNADVVKVL AATGAFRLVQ EAIDKVIEDI KAGKQPELPQ IVVTAEKAVE AGKFSNPYAK AKAMAAFYIA EKVADIDVKG CFIEKDPEKY IPLVASAHEM MRIAAILADQ AREIEKSNDT VFRNPHAKDG KILGKTQLMA KPE //