MTDA_METEA
ID MTDA_METEA Reviewed; 288 AA.
AC P55818; C5B108;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Bifunctional protein MdtA {ECO:0000305};
DE Includes:
DE RecName: Full=NADP-dependent methylenetetrahydromethanopterin dehydrogenase {ECO:0000303|PubMed:9765566};
DE EC=1.5.1.- {ECO:0000269|PubMed:9765566};
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000303|PubMed:8144463};
DE EC=1.5.1.5 {ECO:0000269|PubMed:8144463, ECO:0000269|PubMed:9765566};
GN Name=mtdA {ECO:0000303|PubMed:8144463};
GN OrderedLocusNames=MexAM1_META1p1728;
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], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=8144463; DOI=10.1128/jb.176.7.1957-1968.1994;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Genetics of the serine cycle in Methylobacterium extorquens AM1:
RT identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA.";
RL J. Bacteriol. 176:1957-1968(1994).
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 PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=9765566; DOI=10.1128/jb.180.20.5351-5356.1998;
RA Vorholt J.A., Chistoserdova L.V., Lidstrom M.E., Thauer R.K.;
RT "The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in
RT Methylobacterium extorquens AM1.";
RL J. Bacteriol. 180:5351-5356(1998).
RN [4]
RP STRUCTURE BY NMR IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=11297742; DOI=10.1016/s0014-5793(01)02306-7;
RA Hagemeier C.H., Bartoschek S., Griesinger C., Thauer R.K., Vorholt J.A.;
RT "Re-face stereospecificity of NADP dependent
RT methylenetetrahydromethanopterin dehydrogenase from Methylobacterium
RT extorquens AM1 as determined by NMR spectroscopy.";
RL FEBS Lett. 494:95-98(2001).
CC -!- FUNCTION: Catalyzes the dehydrogenation of methylene-H(4)MPT. Can also
CC catalyze the reversible dehydrogenation of methylene-H(4)F with 20-fold
CC lower catalytic efficiency. {ECO:0000269|PubMed:9765566}.
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 Evidence={ECO:0000269|PubMed:9765566};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:8144463,
CC ECO:0000269|PubMed:9765566};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 mM for methylenetetrahydromethanopterin
CC {ECO:0000269|PubMed:9765566};
CC KM=30 mM for methylenetetrahydrofolate {ECO:0000269|PubMed:9765566};
CC KM=30 mM for NADP(+) (in the presence of
CC methylenetetrahydromethanopterin) {ECO:0000269|PubMed:9765566};
CC KM=10 mM for NADP(+) (in the presence of methylenetetrahydrofolate)
CC {ECO:0000269|PubMed:9765566};
CC Vmax=600 umol/min/mg enzyme with methylenetetrahydromethanopterin as
CC substrate {ECO:0000269|PubMed:9765566};
CC Vmax=30 umol/min/mg enzyme with methylenetetrahydrofolate as
CC substrate {ECO:0000269|PubMed:9765566};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:9765566};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:9765566};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (H(4)MPT route): step 2/5. {ECO:0000269|PubMed:9765566}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11297742}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; L27235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001510; ACS39572.1; -; Genomic_DNA.
DR RefSeq; WP_003597637.1; NC_012988.1.
DR PDB; 1LU9; X-ray; 1.90 A; A/B/C=2-288.
DR PDB; 1LUA; X-ray; 1.90 A; A/B/C=2-288.
DR PDB; 6TGE; X-ray; 1.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-288.
DR PDB; 6TLK; X-ray; 1.80 A; A/B/C/D/E/F=1-288.
DR PDB; 6TM3; X-ray; 1.08 A; A=1-288.
DR PDBsum; 1LU9; -.
DR PDBsum; 1LUA; -.
DR PDBsum; 6TGE; -.
DR PDBsum; 6TLK; -.
DR PDBsum; 6TM3; -.
DR AlphaFoldDB; P55818; -.
DR SMR; P55818; -.
DR STRING; 272630.MexAM1_META1p1728; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR EnsemblBacteria; ACS39572; ACS39572; MexAM1_META1p1728.
DR KEGG; mea:Mex_1p1728; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_059363_0_0_5; -.
DR OMA; LLYQFDT; -.
DR OrthoDB; 1479076at2; -.
DR BioCyc; MetaCyc:MON-3941; -.
DR UniPathway; UPA00562; UER00702.
DR EvolutionaryTrace; P55818; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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 3D-structure; Cytoplasm; Direct protein sequencing; NADP;
KW One-carbon metabolism; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9765566"
FT CHAIN 2..288
FT /note="Bifunctional protein MdtA"
FT /id="PRO_0000199320"
FT BINDING 129..132
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11297742"
FT BINDING 152..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11297742"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11297742"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11297742"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6TM3"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6TM3"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:6TM3"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6TM3"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 249..267
FT /evidence="ECO:0007829|PDB:6TM3"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6TM3"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:6TM3"
SQ SEQUENCE 288 AA; 29736 MW; 36519D60F8F8E830 CRC64;
MSKKLLFQFD TDATPSVFDV VVGYDGGADH ITGYGNVTPD NVGAYVDGTI YTRGGKEKQS
TAIFVGGGDM AAGERVFEAV KKRFFGPFRV SCMLDSNGSN TTAAAGVALV VKAAGGSVKG
KKAVVLAGTG PVGMRSAALL AGEGAEVVLC GRKLDKAQAA ADSVNKRFKV NVTAAETADD
ASRAEAVKGA HFVFTAGAIG LELLPQAAWQ NESSIEIVAD YNAQPPLGIG GIDATDKGKE
YGGKRAFGAL GIGGLKLKLH RACIAKLFES SEGVFDAEEI YKLAKEMA
