ID A0A073JX16_9BACI Unreviewed; 611 AA.
AC A0A073JX16;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Homocysteine methyltransferase {ECO:0000313|EMBL:KEK19539.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:KEK19539.1};
GN ORFNames=BAMA_22365 {ECO:0000313|EMBL:KEK19539.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK19539.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK19539.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK19539.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-2014) 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:KEK19539.1}.
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DR EMBL; JOTN01000007; KEK19539.1; -; Genomic_DNA.
DR RefSeq; WP_034638867.1; NZ_JOTN01000007.1.
DR AlphaFoldDB; A0A073JX16; -.
DR STRING; 574376.BAMA_22365; -.
DR eggNOG; COG0646; Bacteria.
DR eggNOG; COG0685; Bacteria.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000027822; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000027822};
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 611 AA; 67374 MW; AE329FD33DF0B31F CRC64;
MKLLDLLNKG IVIGDGAVGT LLHSHGLQSC FEELNLSDPN RIVSIHKQYV AAGADIIQTN
TYGANEGKLR MYGLENKVEK INKEAVKLAK AAVKERNAVV GTIGGMKHLG AITTTDTERE
FMLLEQANAL LEEGVDGLLL ETFYDEFELL HAVKTLRKQT NIPLIAQLAL HEVGTTQNGN
YIDDILQQLI HVGANVVGLN CQLGPLHMIE SLKMISIPKS GFISAYPNAG LPKYVEGRYE
YEGSVAYFEE TAPKFIEEGV RLLGGCCGTR PAHIEAIKRA LEKKVPITEK QVAERPKIVT
PQRSNVVNRI TLAEKAKKET TIVVELDPPK TLDTNRFFEG AKALKRAGTD AITLADNSLA
SPRISNMAMG SLLTKHDIPV LTHLTCRDHN VIGLQSHLLG LSTLGMEEVL ALTGDPARVG
DFPGATSVYD LSSIELIKMI QEMNNGRSIM GKSIGPATSF SIGAAFNPNV KKLNAAVKRM
ERKIAAGATY FLTQPVYDVA LIEKIYEETK HLEEPIFIGI MPLISKRNAD FLHYEVPGIT
LPEEVRQRMD GHETKESAVQ EGIRIAEELI DVTMKYFNGI YLITPFLRYE VTASLVKYVK
RKQKEKEGIY A
//
