DMRA_METEA
ID DMRA_METEA Reviewed; 135 AA.
AC C5B2R8; Q8KQF4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Dihydromethanopterin reductase;
DE EC=1.5.1.47;
DE AltName: Full=H(2)MPT reductase;
GN Name=dmrA; OrderedLocusNames=MexAM1_META1p4312;
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], DISRUPTION PHENOTYPE, FUNCTION, AND GENE
RP NAME.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=12511515; DOI=10.1128/jb.185.2.669-673.2003;
RA Marx C.J., O'Brien B.N., Breezee J., Lidstrom M.E.;
RT "Novel methylotrophy genes of Methylobacterium extorquens AM1 identified by
RT using transposon mutagenesis including a putative dihydromethanopterin
RT reductase.";
RL J. Bacteriol. 185:669-673(2003).
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=15028691; DOI=10.1128/jb.186.7.2068-2073.2004;
RA Caccamo M.A., Malone C.S., Rasche M.E.;
RT "Biochemical characterization of a dihydromethanopterin reductase involved
RT in tetrahydromethanopterin biosynthesis in Methylobacterium extorquens
RT AM1.";
RL J. Bacteriol. 186:2068-2073(2004).
CC -!- FUNCTION: Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to
CC tetrahydromethanopterin (H(4)MPT). Shows preference for NADPH rather
CC than NADH as electron donor. Does not reduce dihydrofolate.
CC {ECO:0000269|PubMed:12511515, ECO:0000269|PubMed:15028691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + NAD(+) = 7,8-
CC dihydromethanopterin + H(+) + NADH; Xref=Rhea:RHEA:35823,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58103, ChEBI:CHEBI:72788; EC=1.5.1.47;
CC Evidence={ECO:0000269|PubMed:15028691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + NADP(+) = 7,8-
CC dihydromethanopterin + H(+) + NADPH; Xref=Rhea:RHEA:35819,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58103,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:72788; EC=1.5.1.47;
CC Evidence={ECO:0000269|PubMed:15028691};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:15028691};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius (at pH 5.3).
CC {ECO:0000269|PubMed:15028691};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000269|PubMed:15028691}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15028691}.
CC -!- DISRUPTION PHENOTYPE: Mutants have a C1-defective and methanol-
CC sensitive phenotype. {ECO:0000269|PubMed:12511515}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY093431; AAM19724.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS41948.1; -; Genomic_DNA.
DR RefSeq; WP_003606487.1; NC_012988.1.
DR AlphaFoldDB; C5B2R8; -.
DR SMR; C5B2R8; -.
DR STRING; 272630.MexAM1_META1p4312; -.
DR EnsemblBacteria; ACS41948; ACS41948; MexAM1_META1p4312.
DR KEGG; mea:Mex_1p4312; -.
DR eggNOG; COG0262; Bacteria.
DR HOGENOM; CLU_1872632_0_0_5; -.
DR OMA; LRSHMDP; -.
DR OrthoDB; 1920912at2; -.
DR BioCyc; MetaCyc:MON-18688; -.
DR BRENDA; 1.5.1.47; 3296.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR001796; DHFR_dom.
DR Pfam; PF00186; DHFR_1; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..135
FT /note="Dihydromethanopterin reductase"
FT /id="PRO_0000424083"
FT BINDING 9
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 16..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 52..54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 93..97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 135 AA; 15222 MW; A00C054D51CA5E5D CRC64;
MIDVRCICAI GQRGQLGLNG HLPWEGNTDP LFVEDVTRFF ALTMGHVLIA GPKTVASVPE
FAFKDRTIDV IRSHEDPEAV LKRYPGRRIF VGGGIAVWNV YAKYIQHWDV TRLPYDGEAD
RWFDPAWLVG GPLRS
