METF_SPHSK
ID METF_SPHSK Reviewed; 288 AA.
AC G2IQS8; Q60FX0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=5,10-methylenetetrahydrofolate reductase {ECO:0000303|Ref.3};
DE EC=1.5.1.20 {ECO:0000250|UniProtKB:P0AEZ1};
GN Name=metF {ECO:0000303|Ref.3};
GN ORFNames=SLG_12750 {ECO:0000312|EMBL:BAK65950.1};
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=15743951; DOI=10.1128/jb.187.6.2030-2037.2005;
RA Abe T., Masai E., Miyauchi K., Katayama Y., Fukuda M.;
RT "A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for
RT catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6.";
RL J. Bacteriol. 187:2030-2037(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=22207743; DOI=10.1128/jb.06254-11;
RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA Yamazaki S., Fujita N.;
RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT lignin-derived biaryls and monoaryls.";
RL J. Bacteriol. 194:534-535(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NBRC 103272 / SYK-6;
RX AGRICOLA=IND23303201;
RA Sonoki T., Otsuka Y., Ikeda S., Masai E., Kajita S., Katayama Y.;
RT "Tetrahydrofolate-dependent vanillate and syringate O-demethylation links
RT tightly to one-carbon metabolic pathway associated with amino acid
RT synthesis and DNA methylation in the lignin metabolism of Sphingomonas
RT paucimobilis SYK-6.";
RL J. Wood Sci. 48:434-439(2002).
CC -!- FUNCTION: Probably catalyzes the conversion of methyl-tetrahydrofolate
CC to methylene-tetrahydrofolate. Required for tetrahydrofolate-dependent
CC vanillate and syringate O-demethylation. {ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH;
CC Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20;
CC Evidence={ECO:0000250|UniProtKB:P0AEZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH;
CC Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.20;
CC Evidence={ECO:0000250|UniProtKB:P0AEZ1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0AEZ1};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:P0AEZ1}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot grow on vanillate or syringate as
CC the sole source of carbon. Mutant retains vanillate and syringate O-
CC demethylation activity, but accumulates methyl-tetrahydrofolate.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; AB186750; BAD61060.1; -; Genomic_DNA.
DR EMBL; AP012222; BAK65950.1; -; Genomic_DNA.
DR RefSeq; WP_014075601.1; NC_015976.1.
DR AlphaFoldDB; G2IQS8; -.
DR SMR; G2IQS8; -.
DR STRING; 627192.SLG_12750; -.
DR EnsemblBacteria; BAK65950; BAK65950; SLG_12750.
DR KEGG; ssy:SLG_12750; -.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_081788_0_0_5; -.
DR OrthoDB; 1425269at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001275; Chromosome.
DR GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR GO; GO:0106313; F:methylenetetrahydrofolate reductase NADPH activity; IEA:RHEA.
DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR Pfam; PF02219; MTHFR; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..288
FT /note="5,10-methylenetetrahydrofolate reductase"
FT /id="PRO_0000447132"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 46..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 105..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 114..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AEZ1"
SQ SEQUENCE 288 AA; 31367 MW; 237086A7D6679013 CRC64;
MATATLDKAA LSRLFTDYSL EITPKDVEAL ENAAHMIPPG TLISVTFLPG AEYEDRARAA
KRIQELGFRP VPHLSARRLI DEADLRTYLD MLKGVIDLKH VFVIAGDPNE PLGIYEDALA
LIDSGILKEY GIEHCGISGY PEGHPDITDE KLAKAMHDKV ASLKRQGIDY SIMTQFGFDA
EPVLEWLKQI RSEGIDGPVR IGLAGPASIK TLLRFAARCG VGTSAKVVKK YGLSITSLIG
SAGPDPVIED LTPVLGPEHG QVHLHFYPFG GLVKTNEWIV NFKGKQGI
