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Database: UniProt
Entry: A0A0H0XLF2_9SPHN
LinkDB: A0A0H0XLF2_9SPHN
Original site: A0A0H0XLF2_9SPHN 
ID   A0A0H0XLF2_9SPHN        Unreviewed;       318 AA.
AC   A0A0H0XLF2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN   ORFNames=AAV99_10980 {ECO:0000313|EMBL:KLI63194.1};
OS   Aurantiacibacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI63194.1, ECO:0000313|Proteomes:UP000053455};
RN   [1] {ECO:0000313|EMBL:KLI63194.1, ECO:0000313|Proteomes:UP000053455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI63194.1,
RC   ECO:0000313|Proteomes:UP000053455};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL   Submitted (APR-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:KLI63194.1}.
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DR   EMBL; LBHU01000003; KLI63194.1; -; Genomic_DNA.
DR   RefSeq; WP_047094088.1; NZ_LDCP01000003.1.
DR   AlphaFoldDB; A0A0H0XLF2; -.
DR   STRING; 874156.GCA_001021555_02239; -.
DR   PATRIC; fig|874156.12.peg.2253; -.
DR   OrthoDB; 9812555at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000053455; 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:UP000053455}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  34523 MW;  861966F5ECFA9637 CRC64;
     MSVQAPDCLD PVQEKRTARD TPLFSGLPGD IAVSFEFFPP KTDKMEEKLW EAVQELAPLA
     PEFVSVTYGA GGSTRERTHN TVARLIKEAG IPAAAHLTCV DASKAETRAI AEAYWEAGVR
     HIVALRGDAG EPGAPFVPHP EGYANAAELV SGLKEVADFE ISVAAYPETH PDAQCPQSDL
     DNLKRKIDAG ATRGISQFFF APEVFFDFTD KCRAAGIHAP MVPGILPVTN VAQARKFAGQ
     CGAVIPDWMD GLFEGLDERP AARQLVAATI AAELCRRLYA GGVRQFHFYT LNRADLAYAI
     CHMLGRRPVE RGPMEKKS
//
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