ID A0A1Q5XRF7_9BACL Unreviewed; 624 AA.
AC A0A1Q5XRF7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Bifunctional homocysteine S-methyltransferase/methylenetetrahydrofolate reductase {ECO:0000313|EMBL:OKP96905.1};
GN ORFNames=A3849_18765 {ECO:0000313|EMBL:OKP96905.1};
OS Paenibacillus sp. P46E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1349436 {ECO:0000313|EMBL:OKP96905.1, ECO:0000313|Proteomes:UP000185715};
RN [1] {ECO:0000313|EMBL:OKP96905.1, ECO:0000313|Proteomes:UP000185715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P46E {ECO:0000313|EMBL:OKP96905.1,
RC ECO:0000313|Proteomes:UP000185715};
RA Ploux O.;
RL Submitted (MAR-2016) 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:OKP96905.1}.
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DR EMBL; LVYZ01000050; OKP96905.1; -; Genomic_DNA.
DR RefSeq; WP_074112873.1; NZ_LVYZ01000050.1.
DR AlphaFoldDB; A0A1Q5XRF7; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000185715; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 2..285
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 624 AA; 68673 MW; E20FE977C45D469F CRC64;
MKPDLRSAWK NNVLVGDGAM GTFLYQKGFP VGISYEELNL TSPEVIEDVH RSYIEAGAVL
LESNTYSANY DKLSKFGLEA KVDEINRAGV RIARHAAGET GYVVGAVGSI RAGKRANLSS
TELKRFYAQQ FSALLEEQPD GIMLETFYDV EELHLALRAV RKLSELPVIC QLAVDETART
LDGLTLTEAF HILEQDGADI IGFNCRTGPN GIKRALKSLQ GSLRLPASVY PNAGIADYVD
GQYRYGASPD YFGQMAPVFA DMGARIIGGC CGTTPQHIAE ISAALREYSP QPLPEPTAQN
NLERLTVQEH LGDNEERDGH EPTLVDLVKE RHTVIVELDP PRDLDIAKFM RGAEALRRAG
ADALTLADNS LAVTRMSNMA LGHLVQARTG LRPLVHIACR DRNLIGTQSH LMGFDALGID
HVLAVTGDPA RFGDLPGSSS IYDLTSFEII RMIKQLNDGI AFSGKPLKQN ANFVIGAAFN
PNVKHLDKAV ERLEKKIASG ADYIMTQPVY DPELIERIAK ATAHLEIPIF IGIMPLASGR
NAEYLHNEVP GIQLSPEVRS RMQGLEGEEG RAEGVRIAKE LLDAATRHFN GIYLMTPFMF
YDMSVQLLEY VWEKQGRKLS PLFR
//
