ID A1AMZ4_PELPD Unreviewed; 290 AA.
AC A1AMZ4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN OrderedLocusNames=Ppro_1089 {ECO:0000313|EMBL:ABK98714.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98714.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK98714.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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; CP000482; ABK98714.1; -; Genomic_DNA.
DR RefSeq; WP_011735018.1; NC_008609.1.
DR AlphaFoldDB; A1AMZ4; -.
DR STRING; 338966.Ppro_1089; -.
DR KEGG; ppd:Ppro_1089; -.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_025841_0_0_7; -.
DR OrthoDB; 9812555at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006732; 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:UP000006732}.
SQ SEQUENCE 290 AA; 31487 MW; 5009E787C073A404 CRC64;
MRIADLIATR SPFVSLEFFP PKERSEWPAF FQAVEQLAQV DPLFVSVTYG AGGSTQSDTL
EIVSRLTRNL GLEAMAHLTC VGATPEAILE FLNQLSAAGV RNVLALRGDP PKDAPDNFLS
CHSLQYASDL VAYIRSVHPE LGLGVAGYPE THPQAKSPQS DLDFLRLKLD NGGDFVITQL
FFDNTSYFDF VRRARDQGIE KPIIPGIIPV VSLKVIQRIV SLCGATIPAR FLAELEQADR
DGGAAAVREA GVAHARRQAE ELLAGGAPGI HIYTLNRADV VLELTRGLIP
//
