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Database: UniProt
Entry: A0A0P0P0M8_9CAUL
LinkDB: A0A0P0P0M8_9CAUL
Original site: A0A0P0P0M8_9CAUL 
ID   A0A0P0P0M8_9CAUL        Unreviewed;       319 AA.
AC   A0A0P0P0M8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN   ORFNames=AQ619_12030 {ECO:0000313|EMBL:ALL14009.1};
OS   Caulobacter henricii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL14009.1, ECO:0000313|Proteomes:UP000056905};
RN   [1] {ECO:0000313|EMBL:ALL14009.1, ECO:0000313|Proteomes:UP000056905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB4 {ECO:0000313|EMBL:ALL14009.1,
RC   ECO:0000313|Proteomes:UP000056905};
RA   Scott D., Ely B.;
RT   "Conservation of the essential genome among Caulobacter and Brevundimonas
RT   species.";
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}.
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DR   EMBL; CP013002; ALL14009.1; -; Genomic_DNA.
DR   RefSeq; WP_062147790.1; NZ_CP013002.1.
DR   AlphaFoldDB; A0A0P0P0M8; -.
DR   STRING; 69395.AQ619_12030; -.
DR   KEGG; chq:AQ619_12030; -.
DR   eggNOG; COG0685; Bacteria.
DR   OrthoDB; 9812555at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000056905; 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:InterPro.
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}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  34799 MW;  BAE00238FD8ABDA9 CRC64;
     MTLPPARRVI GPVARAGERG QSQAGGRPRV SFEFFPPKTP AMEESLWQAI TRLAPLDPAF
     VSVTYGAGGS TRERTHRTVK RILDETHLKP AAHLTCVGAS RDEVDEVIRE YWQTGVRHIV
     SLRGDPPPTE GGIGGVYVPR ADGYANATEL TQAVRGIAPF EVLVGVYPEK HPESPSIQHD
     IEVLKAKVDA GATLAISQFF FDIDAFLRFV DQVRAAGITI PILPGIMPVT NFNGLKKMSV
     ACQTAVPTWL ANLFEGLDND ADTRRLIACS VAAEMCAKLQ EQGFEDFHFY TLNRADLVYA
     ICRVLGVRER ETAGSEVAA
//
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