ID A0A1F8QW12_9CHLR Unreviewed; 650 AA.
AC A0A1F8QW12;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Hcy-binding domain-containing protein {ECO:0000259|PROSITE:PS50970};
GN ORFNames=A2Z03_07450 {ECO:0000313|EMBL:OGO39647.1};
OS Chloroflexi bacterium RBG_16_56_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797650 {ECO:0000313|EMBL:OGO39647.1, ECO:0000313|Proteomes:UP000177435};
RN [1] {ECO:0000313|EMBL:OGO39647.1, ECO:0000313|Proteomes:UP000177435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO39647.1}.
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DR EMBL; MGNR01000075; OGO39647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8QW12; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000177435; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 2..315
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 650 AA; 70677 MW; 0336D4FFFBF8AC90 CRC64;
MTHPLLDRLA RGPILCDGAM GTLLYARGIS FERCFDELNL SNPALVLEIH GDYIHAGAEM
IETNTFGANR FKLAHHGLEK KVREINLRGV KLAREAREIA GEATFVLGAV GPIGQLLVPL
GQITYADAHA AFKEQIEALL EGGADAIILE TFSDLNELKT AVTAAREVTR DLPLFAQMSF
TDDAHTLTGN TPEEIVAALC ELPVDVIGAN CSVGPAGTFH AVRRMTAALS KSEVGSGKFE
VKPYTSHLAL PTSHFLSVMP NAGFPARIAE RYMYLSSPQY FAEYTPKFVG ELGATIIGGC
CGTTPAHIAA MRDALELIVP TTERRVTNVT SVVVVEKLQA RPPEALTHEL ASVPRTLREK
LRAGKWVTSV ELDPPRGLNP TKMLQGAAML KELGVDAINI GDSPLAKIRM SCISLAIMIQ
QQFGLETIIH YTTRDRNLMA MQSDLIGAHA LGIHNVIALT GDPPRLGDYP NATAVYDIDS
IGLIKILKRL NQGRDWAGTS IGTNADFFVA CALDMMWANS DPNEIDRFHR KLEAGADFVM
TQPIYDAAIL REFLQKYGDK YGAIAEPIIL GVLPLMSAKH AEFLHNEVPG ITLTDEARRR
MKGAGDRGVE EGIKLAQELL TQAKDLVAGT YLMPSFGRYE VCGELVKLVN
//
