ID A0A142L0Q6_9BACT Unreviewed; 334 AA.
AC A0A142L0Q6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AMS25802.1};
GN ORFNames=AEM51_01055 {ECO:0000313|EMBL:AMS25802.1};
OS Bacteroidetes bacterium UKL13-3.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS25802.1, ECO:0000313|Proteomes:UP000075224};
RN [1] {ECO:0000313|Proteomes:UP000075224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037505-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037505-2};
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP012155; AMS25802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142L0Q6; -.
DR STRING; 1690483.AEM51_01055; -.
DR KEGG; bbau:AEM51_01055; -.
DR PATRIC; fig|1690483.4.peg.228; -.
DR Proteomes; UP000075224; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 2.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037505-2};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000075224};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Zinc {ECO:0000256|PIRSR:PIRSR037505-2, ECO:0000256|PROSITE-
KW ProRule:PRU00333}.
FT DOMAIN 1..320
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037505-2,
FT ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 334 AA; 36742 MW; 39995AAB51B43C5A CRC64;
MLITDQLHKR ILILDGAMGT MIQRYQLDEN DFRNEQLKNH PKPLKGNNDL LSITRPEIIK
AIHAQYFDAG ADIIETNTFS GTTIAQADYG LEDWVYEINF QSAKIAREVA DEYTAKNPDK
PRFVAGSMGP TNKTASISPD VNDPGFRGIT FDELVVAFKQ QCKALIEGGV DILLFETIID
TLNAKAALYA AQELFDEMGK KYPIMISGTI TDASGRTLSG QTTEAFLISM EHIPLLSIGL
NCALGAEALR PYLQVLASKS NFFVSAYPNA GLPNEMGQYD QSPNAMMKQV EEFCKEGLVN
ILGGCCGTTP DHIKAIADMA AKYEPRKLHM AMSN
//
