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Database: UniProt
Entry: A0A0C2RDA5_9BACL
LinkDB: A0A0C2RDA5_9BACL
Original site: A0A0C2RDA5_9BACL 
ID   A0A0C2RDA5_9BACL        Unreviewed;       620 AA.
AC   A0A0C2RDA5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=5,10-methylenetetrahydrofolate reductase {ECO:0000313|EMBL:KIL48260.1};
GN   ORFNames=KP78_17070 {ECO:0000313|EMBL:KIL48260.1};
OS   Jeotgalibacillus soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL48260.1, ECO:0000313|Proteomes:UP000031938};
RN   [1] {ECO:0000313|EMBL:KIL48260.1, ECO:0000313|Proteomes:UP000031938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P9 {ECO:0000313|EMBL:KIL48260.1,
RC   ECO:0000313|Proteomes:UP000031938};
RA   Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT   "Genome sequencing of Jeotgalibacillus soli.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIL48260.1}.
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DR   EMBL; JXRP01000013; KIL48260.1; -; Genomic_DNA.
DR   RefSeq; WP_041087872.1; NZ_JXRP01000013.1.
DR   AlphaFoldDB; A0A0C2RDA5; -.
DR   STRING; 889306.KP78_17070; -.
DR   PATRIC; fig|889306.3.peg.1715; -.
DR   OrthoDB; 9803687at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000031938; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; 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   Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003726; HCY_dom.
DR   InterPro; IPR036589; HCY_dom_sf.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   PANTHER; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR11103; SLR1189 PROTEIN; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR   SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR   PROSITE; PS50970; HCY; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031938};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT   DOMAIN          1..281
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50970"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   620 AA;  68335 MW;  F929858D39D4FC4A CRC64;
     MKLIDALQER ILIADGAMGT LLYSYGTDQC FEELNLSAAE HIQQIHTAYI QAGANVIQTN
     TYAGNYHKLE RYGLEDYVKE INRAGVKNAR QAALADTFVV GTIGGIRSLN PQTVKLEEIK
     RSFREQLYCL LLEGVDGILL ETYYDLEELS TVVSIARKET DIPIIAQASL QEVGVLQDGT
     PITEAFKQLE DLGADLVGLN CRLGPYHMLR TLEGVPLPKH AFLSSYPNAS LPSYSDGALQ
     YNNNAEYFRE VAHSFQTQGV RLLGGCCGTT PDHIRAFSEA LKGAVPVLEK DVYIQQPKIE
     VSSRRIYVPE PLQNIVTKRS SIIVELDPPK KLNIDAFMKG AKALKEAGAD AVTLADNSLA
     SPRVSNESLG HLIKAEHDVR PLVHITCRDR NLIGLQSHLM GLHTLGLHDV LAVTGDPTKV
     GDFPGATSVY DVSSFELIEM IQQLNRGVSM SGKDLGESTS FSIGAAFNPN VRSVERAVLR
     MEKKIKAGAD YFMSQPVFSE EKLLEVYEYV KDINAPLYIG LMPLTNSRNA DFLHHEVPGI
     KLSDQVRERM ATVAGDKERS SQEGLAIAKS LIDTALELFN GIYLITPFMR YDLTVELTKY
     AKQQAAKRAG GVNHVSNIIH
//
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