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Database: UniProt
Entry: A0A097QWW0_HAFAL
LinkDB: A0A097QWW0_HAFAL
Original site: A0A097QWW0_HAFAL 
ID   A0A097QWW0_HAFAL        Unreviewed;       302 AA.
AC   A0A097QWW0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:AIU70948.1};
GN   ORFNames=AT03_00040 {ECO:0000313|EMBL:AIU70948.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU70948.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU70948.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU70948.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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; CP009706; AIU70948.1; -; Genomic_DNA.
DR   RefSeq; WP_025799618.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097QWW0; -.
DR   GeneID; 78452618; -.
DR   KEGG; hav:AT03_00040; -.
DR   PATRIC; fig|1453496.5.peg.13; -.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_025841_0_0_6; -.
DR   OrthoDB; 9812555at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000029986; Chromosome.
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:UP000029986}.
SQ   SEQUENCE   302 AA;  33949 MW;  2A2B9CFF699074A2 CRC64;
     MSFFHANQRE ALNQSLAELH GQINVSFEFF PPRTSEMEDT LWQSIDRLSS LKPKFVSVTY
     GANSGERDRT HSIIKGIKDR TGLEAAPHLT CVDATRDELR TIAQDYWNNG IRHIVALRGD
     LPAGGGKPDM YACDLVSLLK EVGDFDISVA AYPEVHPEAK SPQADLINLK RKIDAGANRA
     ITQFFFDVES YLRFRDRCVA TGIDVEIVPG ILPVSNFKQL QRFATMTNVR VPHWMTSMFE
     GLDDDAETRK MVGANIAMDM VKILSREGVK DFHFYTLNRA EMSYAICHTL GVRPEVHSPI
     IA
//
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