BHMT1_PIG
ID BHMT1_PIG Reviewed; 278 AA.
AC Q95332;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Betaine--homocysteine S-methyltransferase 1 {ECO:0000303|PubMed:8798461};
DE EC=2.1.1.5 {ECO:0000269|PubMed:8798461};
DE Flags: Fragment;
GN Name=BHMT {ECO:0000303|PubMed:8798461};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-273, PROTEIN SEQUENCE OF 2-22 AND 257-278,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC TISSUE=Liver;
RX PubMed=8798461; DOI=10.1074/jbc.271.37.22831;
RA Garrow T.A.;
RT "Purification, kinetic properties, and cDNA cloning of mammalian betaine-
RT homocysteine methyltransferase.";
RL J. Biol. Chem. 271:22831-22838(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=9281325; DOI=10.1006/abbi.1997.0246;
RA Sunden S.L.F., Renduchintala M.S., Park E.I., Miklasz S.D., Garrow T.A.;
RT "Betaine-homocysteine methyltransferase expression in porcine and human
RT tissues and chromosomal localization of the human gene.";
RL Arch. Biochem. Biophys. 345:171-174(1997).
CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism.
CC Converts betaine and homocysteine to dimethylglycine and methionine,
CC respectively. This reaction is also required for the irreversible
CC oxidation of choline. {ECO:0000269|PubMed:8798461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine betaine + L-homocysteine = L-methionine + N,N-
CC dimethylglycine; Xref=Rhea:RHEA:22336, ChEBI:CHEBI:17750,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58251; EC=2.1.1.5;
CC Evidence={ECO:0000269|PubMed:8798461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22337;
CC Evidence={ECO:0000305|PubMed:8798461};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by dimethylglycine and
CC methylthioacetate. {ECO:0000269|PubMed:8798461}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for glycine betaine {ECO:0000269|PubMed:8798461};
CC KM=32 uM for L-homocysteine {ECO:0000269|PubMed:8798461};
CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation;
CC sarcosine from betaine: step 1/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O09171}. Nucleus {ECO:0000250|UniProtKB:O09171}.
CC Note=Predominantly localized in the cytoplasm with a small fraction
CC detected in the nucleus. Translocates into the nucleus upon oxidative
CC stress. {ECO:0000250|UniProtKB:O09171}.
CC -!- TISSUE SPECIFICITY: Found exclusively in liver and kidney.
CC {ECO:0000269|PubMed:9281325}.
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DR EMBL; U53421; AAC48632.1; -; mRNA.
DR AlphaFoldDB; Q95332; -.
DR SMR; Q95332; -.
DR MINT; Q95332; -.
DR STRING; 9823.ENSSSCP00000015001; -.
DR PaxDb; Q95332; -.
DR PeptideAtlas; Q95332; -.
DR eggNOG; KOG1579; Eukaryota.
DR HOGENOM; CLU_047457_0_0_1; -.
DR InParanoid; Q95332; -.
DR BRENDA; 2.1.1.5; 6170.
DR UniPathway; UPA00051; UER00083.
DR UniPathway; UPA00291; UER00432.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q95332; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071267; P:L-methionine salvage; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR PROSITE; PS50970; HCY; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Metal-binding; Methyltransferase;
KW Nucleus; Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8798461"
FT CHAIN 2..>278
FT /note="Betaine--homocysteine S-methyltransferase 1"
FT /id="PRO_0000114623"
FT DOMAIN 11..>278
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93088,
FT ECO:0000255|PROSITE-ProRule:PRU00333"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT MOD_RES 98
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT MOD_RES 232
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT MOD_RES 241
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT NON_TER 278
SQ SEQUENCE 278 AA; 30134 MW; 58D3CAFEE7294CA3 CRC64;
MAPVGDKKAK KGILERLNSG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH
REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG
GVSQTPSYLS CKSETEVKKV FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP
VAATMCIGPE GDLHGVTPGQ CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLQAAGL
KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATR
