ID J7W2I2_BACCE Unreviewed; 610 AA.
AC J7W2I2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase {ECO:0000313|EMBL:EJP89341.1};
GN ORFNames=IC3_03411 {ECO:0000313|EMBL:EJP89341.1};
OS Bacillus cereus VD142.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=718224 {ECO:0000313|EMBL:EJP89341.1, ECO:0000313|Proteomes:UP000006969};
RN [1] {ECO:0000313|EMBL:EJP89341.1, ECO:0000313|Proteomes:UP000006969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD142 {ECO:0000313|EMBL:EJP89341.1,
RC ECO:0000313|Proteomes:UP000006969};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD142.";
RL Submitted (JAN-2013) 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:EJP89341.1}.
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DR EMBL; AHCL02000017; EJP89341.1; -; Genomic_DNA.
DR RefSeq; WP_002088636.1; NZ_KE150045.1.
DR AlphaFoldDB; J7W2I2; -.
DR PATRIC; fig|718224.3.peg.3485; -.
DR HOGENOM; CLU_453272_0_0_9; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006969; 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; PTHR45833:SF2; BIFUNCTIONAL HOMOCYSTEINE S-METHYLTRANSFERASE_5,10-METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 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 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 610 AA; 67098 MW; D6B1B5A509FDB342 CRC64;
MKLLDLLSKG IVIGDGAVGT LLHSHGLQSS FEELNLSDPD LIISIHKQYV AAGADVIQTN
TYGANEAKLR MYGLENQVVQ INRAAVNIAK ASVTERNAIL GTIGGMKHIG AVTTTDIERE
FMLLEQAGAL LEEQVDGLLL ETFYDEFELL HAVKVLRKQT SIPIVAQLAL HEAGTTQNGN
DVNEILKQLL DYGANVVGLN CQLGPLHMTE AFKMISIPQN GYLSAYPNAG LPNYVEGRYV
YEGSPAYFEE MTPNFIEQGI RLLGGCCGTT PEHIEGMKRA IANVAPVIAK ETIQRPKVVH
THEKRSRAHV TLAEKAKKQT TVVVELDPPK TLDTQRFFEG ARALKRAGAD AITLADNSLA
SPRVSNMAMG ALLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSALGMEEVL ALTGDPARVG
DFPGATSVYD LSSIELIKMI KEMNDGRSIL GKSIGPATRF SVGGAFNPHV RHLKAAVKRM
ERKIDAGAEY FLTQPIYDVA LIEEVYEATK HLEQPIFIGI MPLVSKRNAD FLHFEVPGIT
LPEEIRQRMD GHETKEAAIE EGIRISQELI DAAMKYFNGI YLITPFLKYE ITEHLVKYVR
EKQEVKEGIN
//
