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Entry: A0A0J5S696_9PAST
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ID   A0A0J5S696_9PAST        Unreviewed;       292 AA.
AC   A0A0J5S696;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN   Name=metF {ECO:0000313|EMBL:KMK52387.1};
GN   ORFNames=RO21_01195 {ECO:0000313|EMBL:KMK52387.1};
OS   Muribacter muris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Muribacter.
OX   NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK52387.1, ECO:0000313|Proteomes:UP000036270};
RN   [1] {ECO:0000313|EMBL:KMK52387.1, ECO:0000313|Proteomes:UP000036270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK52387.1,
RC   ECO:0000313|Proteomes:UP000036270};
RA   Christensen H., Nicklas W., Bisgaard M.;
RT   "Reclassification of Actinobacillus muris as Muribacter muris.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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=1.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19823;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU003862};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000256|ARBA:ARBA00034478}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU003862}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006743, ECO:0000256|RuleBase:RU003862}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMK52387.1}.
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DR   EMBL; JWIZ01000004; KMK52387.1; -; Genomic_DNA.
DR   RefSeq; WP_047975977.1; NZ_JWIZ01000004.1.
DR   AlphaFoldDB; A0A0J5S696; -.
DR   STRING; 67855.RO21_01195; -.
DR   PATRIC; fig|67855.3.peg.1412; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000036270; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   NCBIfam; TIGR00676; fadh2; 1.
DR   PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003862};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036270}.
SQ   SEQUENCE   292 AA;  32937 MW;  B99A681154670F4A CRC64;
     MSYAKEIDLL NQSVADLNGN INVSFEFFPP KNEKMENLLW ESIHRLKVLK PKFVSVTYGA
     NSGERDRTHS IVKTIQQQTG IISAPHLTGI DATPDELRQI AQDYWDSGIR HIVALRGDEP
     PGYTKKPFYA SDLVALLKEV ADFDISVAAY PEVHPEAKSA QSDLLYLKQK VDAGANRAIT
     QFFFDIDSYL RFRDRCATVG IDVEIVPGIL PVSNFKQLEK MAKITNVKIP SWMPKMYQGL
     EEDQTIRNLV AASIAIDMVK VLSKEGVKDF HFYTLNRSEL TYAICHTLGV RP
//
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