ID   MTDB_METEA              Reviewed;         297 AA.
AC   O85012; C5B140;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=NAD(P)-dependent methylenetetrahydromethanopterin dehydrogenase;
DE            EC=1.5.1.-;
GN   Name=mtdB; OrderedLocusNames=MexAM1_META1p1761;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9651254; DOI=10.1126/science.281.5373.99;
RA   Chistoserdova L.V., Vorholt J.A., Thauer R.K., Lidstrom M.E.;
RT   "C1 transfer enzymes and coenzymes linking methylotrophic bacteria and
RT   methanogenic Archaea.";
RL   Science 281:99-102(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
RN   [3]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-16.
RX   PubMed=10848995; DOI=10.1046/j.1432-1327.2000.01413.x;
RA   Hagemeier C.H., Chistoserdova L.V., Lidstrom M.E., Thauer R.K.,
RA   Vorholt J.A.;
RT   "Characterization of a second methylene tetrahydromethanopterin
RT   dehydrogenase from Methylobacterium extorquens AM1.";
RL   Eur. J. Biochem. 267:3762-3769(2000).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of methylene-H(4)MPT.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,10-methylenetetrahydromethanopterin + NAD(+) = 5,10-
CC         methenyl-5,6,7,8-tetrahydromethanopterin + NADH;
CC         Xref=Rhea:RHEA:53384, ChEBI:CHEBI:57540, ChEBI:CHEBI:57818,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58337;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,10-methylenetetrahydromethanopterin + NADP(+) = 5,10-
CC         methenyl-5,6,7,8-tetrahydromethanopterin + NADPH;
CC         Xref=Rhea:RHEA:24682, ChEBI:CHEBI:57783, ChEBI:CHEBI:57818,
CC         ChEBI:CHEBI:58337, ChEBI:CHEBI:58349;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0.;
CC       Temperature dependence:
CC         Optimum temperature is 35-40 degrees Celsius.;
CC   -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC       formaldehyde (H(4)MPT route): step 2/5.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: To M.extorquens MtdA. {ECO:0000305}.
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DR   EMBL; AF032114; AAC27020.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS39604.1; -; Genomic_DNA.
DR   RefSeq; WP_003597578.1; NC_012988.1.
DR   AlphaFoldDB; O85012; -.
DR   SMR; O85012; -.
DR   STRING; 272630.MexAM1_META1p1761; -.
DR   EnsemblBacteria; ACS39604; ACS39604; MexAM1_META1p1761.
DR   KEGG; mea:Mex_1p1761; -.
DR   eggNOG; COG0702; Bacteria.
DR   HOGENOM; CLU_059363_0_0_5; -.
DR   OMA; RPYILHM; -.
DR   OrthoDB; 1479076at2; -.
DR   BioCyc; MetaCyc:MON-4042; -.
DR   UniPathway; UPA00562; UER00702.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01078; NAD_bind_H4MPT_DH; 1.
DR   Gene3D; 3.40.50.10280; -; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR015259; Methyl-teptahyd_DH_N.
DR   InterPro; IPR037089; Methyl-teptahyd_DH_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR035015; NAD-bd_H4MPT_DH.
DR   Pfam; PF09176; Mpt_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; NADP; One-carbon metabolism;
KW   Oxidoreductase.
FT   CHAIN           1..297
FT                   /note="NAD(P)-dependent methylenetetrahydromethanopterin
FT                   dehydrogenase"
FT                   /id="PRO_0000096616"
SQ   SEQUENCE   297 AA;  31151 MW;  C7134759CAA1ABE8 CRC64;
     MARSILHMLT PLKHMSPFDV NMAIDAGFET LIPYTGVDLT DVVSLTQDSI FSRAPQDGVR
     TGIFIGGKNA ELALDMVDRA KKAFVPPFVN HVFADPAGSF TTGAAMVAEV NRALKARFST
     DLKGKRIVIF GGAGVVAYVA AVIGALEGAQ TVLVGHDGEE RVSKIAFTMK WRFGIDVGAV
     DGTLPEARRA AITDADVILS AGPAGVSILT AEDLESAPKL LVASDVNAVP PAGIAGIDVN
     AVDVPLPTGK GVGIGALAVG NVKYQTQCRM FRKMLEAQEP LCLDFRDAYK LAVEIAG