METF_HAEIN
ID METF_HAEIN Reviewed; 292 AA.
AC P45208;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE EC=1.5.1.20;
GN Name=metF; OrderedLocusNames=HI_1444;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
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; L42023; AAC23094.1; -; Genomic_DNA.
DR PIR; H64123; H64123.
DR RefSeq; NP_439596.1; NC_000907.1.
DR RefSeq; WP_005652747.1; NC_000907.1.
DR PDB; 5UME; X-ray; 2.70 A; A/B/C/D/E/F=1-292.
DR PDBsum; 5UME; -.
DR AlphaFoldDB; P45208; -.
DR SMR; P45208; -.
DR STRING; 71421.HI_1444; -.
DR EnsemblBacteria; AAC23094; AAC23094; HI_1444.
DR KEGG; hin:HI_1444; -.
DR PATRIC; fig|71421.8.peg.1506; -.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_025841_0_0_6; -.
DR OMA; EMHPQAR; -.
DR PhylomeDB; P45208; -.
DR BioCyc; HINF71421:G1GJ1-1470-MON; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IBA:GO_Central.
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:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd00537; MTHFR; 1.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR InterPro; IPR004620; MTHF_reductase_bac.
DR Pfam; PF02219; MTHFR; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
DR TIGRFAMs; TIGR00676; fadh2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; FAD; Flavoprotein;
KW Methionine biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..292
FT /note="5,10-methylenetetrahydrofolate reductase"
FT /id="PRO_0000190263"
FT ACT_SITE 26
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 26..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 57..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 57..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 116..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129..130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 154..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 163..170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:5UME"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 244..264
FT /evidence="ECO:0007829|PDB:5UME"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:5UME"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:5UME"
SQ SEQUENCE 292 AA; 33020 MW; C6DCC9BC80CFF9B4 CRC64;
MSYAKEIDTL NQHIADFNKK INVSFEFFPP KNEKMETLLW DSIHRLKVLK PKFVSVTYGA
NSGERDRTHG IVKAIKQETG LEAAPHLTGI DATPEELKQI ARDYWDSGIR RIVALRGDEP
KGYAKKPFYA SDLVELLRSV ADFDISVAAY PEVHPEAKSA QADLINLKRK IDAGANHVIT
QFFFDIENYL RFRDRCASIG IDTEIVPGIL PVTNFKQLQK MASFTNVKIP AWLVKAYDGL
DNDPTTRNLV AASVAMDMVK ILSREGVNDF HFYTLNRSEL TYAICHMLGV RP