ID S5R0J6_9STRE Unreviewed; 618 AA.
AC S5R0J6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein {ECO:0000313|EMBL:AGS05679.1};
GN ORFNames=KE3_1195 {ECO:0000313|EMBL:AGS05679.1};
OS Streptococcus lutetiensis 033.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05679.1, ECO:0000313|Proteomes:UP000015268};
RN [1] {ECO:0000313|EMBL:AGS05679.1, ECO:0000313|Proteomes:UP000015268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=033 {ECO:0000313|EMBL:AGS05679.1,
RC ECO:0000313|Proteomes:UP000015268};
RX PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA Xu J.;
RT "Dynamics of fecal microbial communities in children with diarrhea of
RT unknown etiology and genomic analysis of associated Streptococcus
RT lutetiensis.";
RL BMC Microbiol. 13:141-141(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}.
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DR EMBL; CP003025; AGS05679.1; -; Genomic_DNA.
DR RefSeq; WP_020916941.1; NC_021900.1.
DR AlphaFoldDB; S5R0J6; -.
DR KEGG; slu:KE3_1195; -.
DR PATRIC; fig|1076934.5.peg.1161; -.
DR HOGENOM; CLU_453272_0_0_9; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000015268; Chromosome.
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 1..287
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 618 AA; 68352 MW; 929145FA58496624 CRC64;
MSRLLERLKT DILVADGAMG TLLYANGLDN CYETYNLTHP EKVLAIHKTY IEAGADVIQT
NTYTAKRHRL DGYGYGEKIK EINQAGVKIA RQAAGEDTFV LGTVGALRGL KQCELTLNEI
IKETLEQVRY LLETEEIDGL LFETYYDEEE IIEVLKVVRP LTDLPIITNI SIHEAGITEN
GRPLVEIFGK LVMLGADVVG LNCHLGPYHM IQSLKQVPLF AQSYLSVYPN ASLLSFVDDN
GSGQYGFSQN ADYFGKSAEL LVAEGARLIG GCCGTTPDHI RAVKRAVKGL KPVSRKFVTP
MVEEAELIKA VKQSETIVDK VERKVTIIAE LDPPKTLDIR KFTKGVKALD EAGVAAITLA
DNSLAKTRIC NVSIASLLKN EISTPFLLHL SCRDHNMIGL QSRLLGMDVL GFHQVLAITG
DPSKIGDFPG ATSVYDATSF KLLELIKQLN KGIGYSGASI KKETTFTAAA AFNPNVKNLS
RCGRLIERKI AAGADCFITQ PIFNSEIIEN LAELTRDYDT PFFVGIMPIT SYNNAIFLHN
EVPGIQLSDD FLAKLEAVKD DKEKCQQLAL EESKQLIDHA LKFFNGIYLI TPFMRYDLTV
DLVEYIHQKV EQSHQIIP
//
