ID Q4L331_STAHJ Unreviewed; 612 AA.
AC Q4L331;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Hcy-binding domain-containing protein {ECO:0000259|PROSITE:PS50970};
GN OrderedLocusNames=SH2637 {ECO:0000313|EMBL:BAE05946.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05946.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE05946.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05946.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05946.1; -; Genomic_DNA.
DR RefSeq; WP_011276876.1; NC_007168.1.
DR AlphaFoldDB; Q4L331; -.
DR KEGG; sha:SH2637; -.
DR eggNOG; COG0646; Bacteria.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_453272_0_0_9; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000543; 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; 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..282
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 202
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"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 612 AA; 67988 MW; 435CE376598E6A96 CRC64;
MSRLLNQLQN NVLVADGAMG TILYSEGLDT CPEAYNLTHP EKVESIHRSY IEAGADIIQT
NTYGANFEKL RRFGLEHKVK DIHKAAVAIA KRAARPDTFI LGTVGGFRSL QQEELPLSTI
QYHAENQIDT LVEEGVDGLL FETYYDLEEL TNIVTTTRRK YDIPIIAQLT ASNTNYLVDG
TEINKALQQL VACGANVVGL NCHHGPHHMQ RSFSHIELPE TAYLSCYPNA SLLDIENSEF
KYSDNAQYFG DVAQELINEG VRLIGGCCGT TPQHIAYIKS SVKDLKPVKN KNVIPINRQT
NRAVTHTYKH NLTTKVKNGP TVIVELDTPK HLDTDLFFEN IGKLDEANID AVTLADNSLA
TVRVSNIAAA SIIRQRYNIE PLVHITCRDR NLIGLQSHLL GLSLIGVNEI LAITGDPSKV
GHLPGATNVY DVNSKGLTEL ALRFNQGINT DGDALKKHTN FNIAGAFDPN VRKLDGAVKR
LEKKVAAGMN YFITQPVYSK EKIKEVYEAT KHLNVPLFIG IMPIASYNNA LFLHNEVPGI
KMSEDVLSQF KAVKDDKEKT KALSLRLSKE LIDTVHEYFN GLYIITPFQR IDYSLELAAY
SKAITQNKEA IS
//
