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Database: UniProt
Entry: Q88D51_PSEPK
LinkDB: Q88D51_PSEPK
Original site: Q88D51_PSEPK 
ID   Q88D51_PSEPK            Unreviewed;       295 AA.
AC   Q88D51;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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:AAN70543.1};
GN   OrderedLocusNames=PP_4977 {ECO:0000313|EMBL:AAN70543.1};
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN70543.1, ECO:0000313|Proteomes:UP000000556};
RN   [1] {ECO:0000313|EMBL:AAN70543.1, ECO:0000313|Proteomes:UP000000556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC   {ECO:0000313|Proteomes:UP000000556};
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA   Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA   Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA   Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA   Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA   Dusterhoft A., Tummler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70543.1; -; Genomic_DNA.
DR   RefSeq; NP_747079.1; NC_002947.4.
DR   AlphaFoldDB; Q88D51; -.
DR   STRING; 160488.PP_4977; -.
DR   PaxDb; 160488-PP_4977; -.
DR   KEGG; ppu:PP_4977; -.
DR   PATRIC; fig|160488.4.peg.5316; -.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_025841_0_0_6; -.
DR   OrthoDB; 9812555at2; -.
DR   PhylomeDB; Q88D51; -.
DR   BioCyc; PPUT160488:G1G01-5322-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000556; 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:UP000000556}.
SQ   SEQUENCE   295 AA;  32980 MW;  DDE6C6CA85DD3CA5 CRC64;
     MQLAARRLLP EERLMSQERR YSFEFFPTKT DAGHEKLMGV ARQLATYNPD FFSCTYGAGG
     STRDRTLNTV LQLESEVKIP AAPHLSCVGD TKAELRALLA EYKAAGIKRI VALRGDLPSG
     MGMASGELRY ASDLVEFIRE ETADHFHLEV AAYPEMHPQA RNFEADLANF VHKVKAGADS
     AITQYFFNAD SYFYFVERAQ KLGVEIPVVP GIMPITNYSK LARFSDACGA EIPRWIRKQL
     EAYADDTASI QAFGEEVITR MCEQLLQGGA PGLHFYTLNQ AEPSLAIWNN LKLPR
//
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