ID U2NNK8_9CLOT Unreviewed; 585 AA.
AC U2NNK8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein {ECO:0000313|EMBL:ERK30758.1};
DE EC=2.1.1.10 {ECO:0000313|EMBL:ERK30758.1};
GN ORFNames=CINTURNW_2464 {ECO:0000313|EMBL:ERK30758.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK30758.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK30758.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK30758.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
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:ERK30758.1}.
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DR EMBL; APJA01000012; ERK30758.1; -; Genomic_DNA.
DR RefSeq; WP_021802453.1; NZ_KI273145.1.
DR AlphaFoldDB; U2NNK8; -.
DR STRING; 1294142.CINTURNW_2464; -.
DR PATRIC; fig|1294142.3.peg.2544; -.
DR eggNOG; COG0646; Bacteria.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_453272_0_0_9; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000016721; 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 Reference proteome {ECO:0000313|Proteomes:UP000016721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 1..274
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 585 AA; 65438 MW; ADF098E690FE3EBF CRC64;
MKTKKKPLIF DGAMGTYYSV LSKNPSTKCE FGNLYDRQTV LDIHKEYIDA GCGAIRTNTF
GANKEALESD FDVVKRVIKE GYEIAKEATK GTSVSVFADI GPIKELEGHE LFKEYQEIVD
VFLDLGADNF IFETFSQEEC LVDICKYIKS KNPKAFILVE FAVSPEGYTR LGNSGKKLID
KLSKITEIDA LGFNCFSGPY HLLQYIKEFN IEDKTISIMP NSGYPTIINN RTFFDNSKEY
FASQMFEIAK LGVSILGGCC GTTPEYIKAM VLKLKELSLD DIVYDKISKP SEIKKSEVKN
KLIEKLDKGE KIIAVELDPP IDTEIDFFMS SAKKLKDQGV DAITIADCPI ARARVDSSIL
ACKLKRELDI TPIPHMTCRD RNINATKALL LGLNIEGVNN VLVVTGDPIP SAERDEVKGV
FSFNSSILAN YITNLNETTF KSPFNVCGAL NINARNFNAQ MVQAKKKIEN GITMFLTQPV
LTKEALENLK LARKELDAKI LGGIIPVVSY RNACFMNNEI SGINVSEEII EMYKDISKEE
GTELAVKLST QIAEEISEYV DGYYLITPFK RIDIISRIIE NIKNK
//
