BHMT1_BOVIN
ID BHMT1_BOVIN Reviewed; 407 AA.
AC Q5I597; Q2KIL0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE EC=2.1.1.5 {ECO:0000250|UniProtKB:Q93088};
GN Name=BHMT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Charest R., Beaudry D., Girard C., Palin M.-F.;
RT "Interactions folic acid-vitamin B12-methionine: effects on liver
RT metabolism and production of dairy cows.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q93088}.
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:0000250|UniProtKB:Q93088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22337;
CC Evidence={ECO:0000250|UniProtKB:Q93088};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q93088};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q93088};
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 {ECO:0000250|UniProtKB:Q93088}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q93088}.
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}.
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DR EMBL; AY854632; AAW39034.1; -; mRNA.
DR EMBL; BC112599; AAI12600.1; -; mRNA.
DR RefSeq; NP_001011679.1; NM_001011679.1.
DR AlphaFoldDB; Q5I597; -.
DR SMR; Q5I597; -.
DR STRING; 9913.ENSBTAP00000002916; -.
DR PaxDb; Q5I597; -.
DR PeptideAtlas; Q5I597; -.
DR PRIDE; Q5I597; -.
DR GeneID; 497025; -.
DR KEGG; bta:497025; -.
DR CTD; 635; -.
DR eggNOG; KOG1579; Eukaryota.
DR HOGENOM; CLU_047457_0_0_1; -.
DR InParanoid; Q5I597; -.
DR OrthoDB; 731388at2759; -.
DR TreeFam; TF329202; -.
DR UniPathway; UPA00051; UER00083.
DR UniPathway; UPA00291; UER00432.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..407
FT /note="Betaine--homocysteine S-methyltransferase 1"
FT /id="PRO_0000236274"
FT DOMAIN 11..314
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 BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93088,
FT ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 300
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 MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09171"
FT MOD_RES 340
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT MOD_RES 377
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35490"
FT CONFLICT 216
FT /note="N -> K (in Ref. 2; AAI12600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 44878 MW; 101C4070BAA30096 CRC64;
MAPAGGKNVK KGILERLNSG EVIIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH
REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN EAACDIARQV ADEGDALVAG
GVSQTPSYLS CKSETEVKKV FQQQLEVFVK KNVDFLIAEY FEHVEEAVWA VEALKASGKP
VAATMCIGPE GDLHSVTPGE CAVRLVKAGA SIVGVNCHFD PTISLQTVKL MKEGLEAAGL
KAHLMSQPLA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC
GFEPYHIRAI AEELAPERGF LPLASEKHGS WGSGLDMHTK PWIRARARKE YWENLQIASG
RPYNPSMSKP DAWGVTKGTA ELMQQKEATT EQQLRELFEK QKFKSAQ
