ID A0A0P6X145_9CHLR Unreviewed; 600 AA.
AC A0A0P6X145;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Hcy-binding domain-containing protein {ECO:0000259|PROSITE:PS50970};
GN ORFNames=ADM99_05620 {ECO:0000313|EMBL:KPL72985.1};
OS Leptolinea tardivitalis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Leptolinea.
OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL72985.1, ECO:0000313|Proteomes:UP000050430};
RN [1] {ECO:0000313|EMBL:KPL72985.1, ECO:0000313|Proteomes:UP000050430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL72985.1,
RC ECO:0000313|Proteomes:UP000050430};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL Submitted (JUL-2015) 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:KPL72985.1}.
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DR EMBL; LGCK01000007; KPL72985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P6X145; -.
DR STRING; 229920.ADM99_05620; -.
DR PATRIC; fig|229920.5.peg.1094; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000050430; 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:UP000050430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 1..273
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 258
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"
SQ SEQUENCE 600 AA; 64993 MW; 3A31018CA3F686F6 CRC64;
MGTMLHQKGV SFDACFDELN ITNPSIVGEI HRDYIEAGSQ IIQTNTFGAN CYKLARFGLG
NRVKEINTAG VDLARRVIQG TFKEILIAGD IGPLGVRLAP YGRVQPEEAR LAFTEQISAL
LDAGVDLLLI ETMTDLQETR LAVKVARSLN QTIPIIASMT FTRDDRTLLG DSPSIVARTL
INEGADLTGV NCSGGPQQIL RILRQMHAAI PNGKFSVMPN AGWPEQVGGR IMYAATPEYF
GDYAVLFHQN GARIIGGCCG TTPEHISAMK KALSKAVPLE SAEPFEVSEQ EPEFSRKEEA
LAPTKFGAKI SAGKFVTAVE MDPPRGLATQ KLIAGASLLA EAGVDVINVA DSPMARMRMS
PWAVCSLIQQ KVGIETVLHF PTRGRNLIRV QGDLLAAHAL DVRNVFVVMG DPTSIGDYPD
AMDNYDLVPS GLIKLIKQGF NTGIDHSGAN IGQPTNFFVG CALNLTPNSP ADEIKNLARK
IKAGADFALT QPVFQPEAAR EFINRIKNEM GEFNLPILGG VLPLANTRHA NFLDQEVPGI
IIPPSVLERM RKAGEKSSEE GVKIAVELIE ELRPLINGAY IMPAFNRYDL VAEVVEAIKE
//
