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Database: UniProt
Entry: A0A101NBG3_9ACTN
LinkDB: A0A101NBG3_9ACTN
Original site: A0A101NBG3_9ACTN 
ID   A0A101NBG3_9ACTN        Unreviewed;       307 AA.
AC   A0A101NBG3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN   ORFNames=AQI94_05340 {ECO:0000313|EMBL:KUM90012.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM90012.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM90012.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM90012.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
RL   Submitted (OCT-2015) 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:KUM90012.1}.
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DR   EMBL; LMWM01000005; KUM90012.1; -; Genomic_DNA.
DR   RefSeq; WP_051832955.1; NZ_KQ948144.1.
DR   AlphaFoldDB; A0A101NBG3; -.
DR   OrthoDB; 9812555at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000053039; 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}.
SQ   SEQUENCE   307 AA;  33407 MW;  8ED8DCC65B7A3575 CRC64;
     MALGTASTRT DRARTVRDML AAGKTTHSFE FSAPKTPKGE RNLWSALRRV EAVAPDFVSV
     TYGAGGSTRA GTVKETQQIV ADTTLTPVAH LTAVNHSIAE LRNIIGQYAD AGIRNILAVR
     GDPPGDPMGD WLAHPQGLTY AAELVQLIKE SGDFCVGVAA FPEMHPRSAD WDTDVARFVD
     KCRAGADYAI TQMFFQPESY LRLRDRVHAA DCETPVIPEV MPVTSVRMLE RLPQLSNASI
     PSALEERILT AKDDPAAVRS IGIEFATEFC ARLLSEGVPG LHFITLNNST ATLEIYENLG
     LHHRPQA
//
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