YITJ_BACSU
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 03-AUG-2022, entry version 122.
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; Firmicutes; 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;
CC Evidence={ECO:0000255|PROSITE-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; O06745; -.
DR PRIDE; O06745; -.
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 OMA; TNTYAAN; -.
DR PhylomeDB; O06745; -.
DR BioCyc; BSUB:BSU11010-MON; -.
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:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
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; 3.20.20.330; -; 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 Pfam; PF02219; MTHFR; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
DR SUPFAM; SSF82282; SSF82282; 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
