ID A0A1I2BCM8_9BACT Unreviewed; 317 AA.
AC A0A1I2BCM8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN ORFNames=DET52_105105 {ECO:0000313|EMBL:TDO01250.1},
GN SAMN05216283_101379 {ECO:0000313|EMBL:SFE53905.1};
OS Sunxiuqinia elliptica.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=655355 {ECO:0000313|EMBL:SFE53905.1, ECO:0000313|Proteomes:UP000198964};
RN [1] {ECO:0000313|EMBL:SFE53905.1, ECO:0000313|Proteomes:UP000198964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFE53905.1,
RC ECO:0000313|Proteomes:UP000198964};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TDO01250.1, ECO:0000313|Proteomes:UP000294848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114D {ECO:0000313|EMBL:TDO01250.1,
RC ECO:0000313|Proteomes:UP000294848};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (MAR-2019) 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}.
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DR EMBL; FONW01000001; SFE53905.1; -; Genomic_DNA.
DR EMBL; SNWI01000005; TDO01250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2BCM8; -.
DR STRING; 655355.SAMN05216283_101379; -.
DR OrthoDB; 9812555at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000198964; Unassembled WGS sequence.
DR Proteomes; UP000294848; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
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:UP000198964}.
SQ SEQUENCE 317 AA; 35394 MW; 8B2609A37B7029F9 CRC64;
MKVIDIINNS DKTVFSFELL PPLKGNDAST IYRTIESLID YAPQYINITT HRDEMIYKEL
ADGSIEKRTV RKRPGTVAIA AAIQHKYGIP VVPHILCGGF SKSETEHVLI DLNFMGISNV
LALRGDGLKS DHVFRANPDG HANASELVEQ IVNLREGKYL EPDLKNNSPL DFCVGVAGYP
EKHFEAPNFD TDMAYLKQKV DAGADYIVTQ MFFDNQVYYN FVDKCREAGI TVPIIPGIKP
INLKNQLTVL PKIFSIDLPQ ELATELAKCK NNDDAKVVGT EWAIYQSKDL VANKVPSLHL
YTYGVSDNAR KIVEAVF
//
