METF_NEIMB
ID METF_NEIMB Reviewed; 292 AA.
AC Q9JZQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE EC=1.5.1.20;
GN Name=metF; OrderedLocusNames=NMB0943;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
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 -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF41349.1; -; Genomic_DNA.
DR PIR; D81140; D81140.
DR RefSeq; NP_273981.1; NC_003112.2.
DR RefSeq; WP_002223857.1; NC_003112.2.
DR AlphaFoldDB; Q9JZQ3; -.
DR SMR; Q9JZQ3; -.
DR STRING; 122586.NMB0943; -.
DR PaxDb; Q9JZQ3; -.
DR EnsemblBacteria; AAF41349; AAF41349; NMB0943.
DR GeneID; 61281160; -.
DR KEGG; nme:NMB0943; -.
DR PATRIC; fig|122586.8.peg.1198; -.
DR HOGENOM; CLU_025841_0_2_4; -.
DR OMA; EMHPQAR; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000425; 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 Amino-acid biosynthesis; FAD; Flavoprotein; Methionine biosynthesis; NAD;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..292
FT /note="5,10-methylenetetrahydrofolate reductase"
FT /id="PRO_0000320271"
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"
SQ SEQUENCE 292 AA; 33056 MW; 32B22282A681CB1F CRC64;
MNYAKEINAL NNSLSDLKGD INVSFEFFPP KNEQMETMLW DSIHRLQTLH PKFVSVTYGA
NSGERDRTHG IVKRIKQETG LEAAPHLTGI DASPDELRQI AKDYWDSGIR RIVALRGDEP
AGYEKKPFYA EDLVKLLRSV ADFDISVAAY PEVHPEAKSA QADLINLKRK IDAGANHVIT
QFFFDVERYL RFRDRCVMLG IDVEIVPGIL PVTNFKQLGK MAQVTNVKIP SWLSQMYEGL
DDDQGTRNLV AASIAIDMVK VLSREGVKDF HFYTLNRSEL TYAICHILGV RP
