ID   M1PJE5_DESSD            Unreviewed;       894 AA.
AC   M1PJE5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
GN   OrderedLocusNames=UWK_03163 {ECO:0000313|EMBL:AGF79690.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79690.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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: 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; CP003985; AGF79690.1; -; Genomic_DNA.
DR   RefSeq; WP_015405374.1; NC_020304.1.
DR   AlphaFoldDB; M1PJE5; -.
DR   STRING; 1167006.UWK_03163; -.
DR   KEGG; dsf:UWK_03163; -.
DR   PATRIC; fig|1167006.5.peg.3409; -.
DR   eggNOG; COG0685; Bacteria.
DR   eggNOG; COG2069; Bacteria.
DR   HOGENOM; CLU_323884_0_0_7; -.
DR   OrthoDB; 5428919at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000011721; Chromosome.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0006555; P:methionine metabolic 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   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF03599; CdhD; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   DOMAIN          599..877
FT                   /note="CO dehydrogenase/acetyl-CoA synthase delta subunit
FT                   TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF03599"
FT   COILED          340..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          489..551
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   894 AA;  94627 MW;  EDEE3AE2CD7847C1 CRC64;
     MKSGSKLETL LKEGTFVVTG ELGPPKNGNP EVVREKAQLL KGNVDAVNIT DCQTAIVRMS
     SIAAGLIAKE EGLEPVIQMT CRDRNRIGMQ SDILGASALG LKNLLCLTGD HQKFGNHPGS
     KGVFDMDSIQ MLGMMKGMRD DKIFQCGEEI KSNEPKLFLG AAANPFAYPF EYRAVRLGKK
     VAAGADFIQT QIIYNVEKFR EFMKMVRDLG LHEKCYILAG VTPPKSLGMA RYMKKFVPGM
     DVTDEVIQRM KDAKDMQDEG IQICADIINE VKDIEGVAGI HCMAIEWESA VPEILKRAGL
     LPRPGITETD AAVKPIATDE VKEQITVQSV DTDTLLEKAK AEAAAIIAAA KAEAENLKQK
     AAAVSSVATA TTSITTEAPQ GVDDSGEHEM NEKERIMALD SVNLGLAALK KAYGLTDDQF
     EALSSFAGAH AILKKEPEVV SSAPVAPVAA AAPQAPAAPA APAAPVIDDS AEKAKAEAAA
     KAKADAEAKA DEEAKLKAAA AAKLKAEAQE KAAADAKAAA DAKAADEAKA KAAAEEKAAA
     EAKVKAEAEA KANVQAAPAP VADSGVGELA KETVSLADRS TKVAPANYET KYSGELRSVK
     LGNEGNEKIV GGSSSMPFHL FEGDHPNKPL IAMEVSDVKP DEWPETLSRH FSDVFDNPVA
     WAEKCVKVYG AEAIAVTLGS TDPNGMNRSA ADAAKTAAAV IAAVDVPVIV WGCGNSDKDT
     ETLRDITSVI GDKKVCLAPL EDSNYRTIGA TAMAFQHPIV AASPIDVNLA KQLNILLENL
     GVSLDTVLMD PSIGALGYGI EYTYSVMERI RIAALTQQDA KLQVPIICNL GCEVWKAKET
     KLPSDDMIGD QETRGIMMEA LTASCMLMAG GEVMIMRHPK AIALTNAMVA GLMD
//