ID   YITJ_BACSU              Reviewed;         612 AA.
AC   O06745; Q796P9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase;
DE   Includes:
DE     RecName: Full=Homocysteine S-methyltransferase;
DE              EC=2.1.1.10;
DE     AltName: Full=S-methylmethionine:homocysteine methyltransferase;
DE   Includes:
DE     RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE              EC=1.5.1.20;
GN   Name=yitJ; OrderedLocusNames=BSU11010;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA   Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT   "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT   position encoding 11 membrane proteins.";
RL   Microbiology 143:3309-3312(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION.
RC   STRAIN=168 / BR151;
RX   PubMed=10094622; DOI=10.1046/j.1365-2958.1998.01105.x;
RA   Grundy F.J., Henkin T.M.;
RT   "The S box regulon: a new global transcription termination control system
RT   for methionine and cysteine biosynthesis genes in Gram-positive bacteria.";
RL   Mol. Microbiol. 30:737-749(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC         methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20;
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=1.5.1.20;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00333};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- INDUCTION: Induced by methionine starvation.
CC       {ECO:0000269|PubMed:10094622}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       methylenetetrahydrofolate reductase family. {ECO:0000305}.
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DR   EMBL; Y09476; CAA70665.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12941.1; -; Genomic_DNA.
DR   PIR; C69840; C69840.
DR   RefSeq; NP_388982.1; NC_000964.3.
DR   RefSeq; WP_003245847.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O06745; -.
DR   SMR; O06745; -.
DR   STRING; 224308.BSU11010; -.
DR   PaxDb; 224308-BSU11010; -.
DR   EnsemblBacteria; CAB12941; CAB12941; BSU_11010.
DR   GeneID; 939796; -.
DR   KEGG; bsu:BSU11010; -.
DR   PATRIC; fig|224308.179.peg.1183; -.
DR   eggNOG; COG0646; Bacteria.
DR   eggNOG; COG0685; Bacteria.
DR   InParanoid; O06745; -.
DR   OrthoDB; 9803687at2; -.
DR   PhylomeDB; O06745; -.
DR   BioCyc; BSUB:BSU11010-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0106313; F:methylenetetrahydrofolate reductase NADPH activity; IEA:RHEA.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; FAD; Flavoprotein; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; NAD; NADP; Oxidoreductase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN           1..612
FT                   /note="Bifunctional homocysteine S-methyltransferase/5,10-
FT                   methylenetetrahydrofolate reductase"
FT                   /id="PRO_0000379125"
FT   DOMAIN          1..280
FT                   /note="Hcy-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   REGION          1..280
FT                   /note="Homocysteine S-methyltransferase"
FT   REGION          295..612
FT                   /note="5,10-methylenetetrahydrofolate reductase"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
SQ   SEQUENCE   612 AA;  67928 MW;  A7B6FFC2E648F800 CRC64;
     MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV EAGANIIQTN
     TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG TMGGIRTFNK NAYSLDEIKR
     SFREQLYLLL HEEPDGLLLE TYYDLEEARE VLKIARKETD LPIMLNVSMH EQGVLQDGTP
     LSDALRSIAD LGADIVGINC RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY
     ETDDTYFQNS ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITEKE VKTRAKEFIS
     VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL TLADNSLATP
     RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL DTLGLNDVLA ITGDPSKIGD
     FPGATSVYDL TSFDLIRLIK QFNEGLSLSG KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE
     KKIDCGADYF VSQPVYSEQQ LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL
     SDTIREKMAH AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ
     QKDEQRQNIF LH
//