BHMT1_PONAB
ID BHMT1_PONAB Reviewed; 406 AA.
AC Q5RFG2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE EC=2.1.1.5 {ECO:0000250|UniProtKB:Q93088};
GN Name=BHMT;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857196; CAH89495.1; -; mRNA.
DR RefSeq; NP_001127156.1; NM_001133684.1.
DR AlphaFoldDB; Q5RFG2; -.
DR SMR; Q5RFG2; -.
DR STRING; 9601.ENSPPYP00000017424; -.
DR Ensembl; ENSPPYT00000018130; ENSPPYP00000017424; ENSPPYG00000015586.
DR GeneID; 100174207; -.
DR KEGG; pon:100174207; -.
DR CTD; 635; -.
DR eggNOG; KOG1579; Eukaryota.
DR GeneTree; ENSGT00390000003122; -.
DR InParanoid; Q5RFG2; -.
DR OrthoDB; 731388at2759; -.
DR UniPathway; UPA00051; UER00083.
DR UniPathway; UPA00291; UER00432.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071267; P:L-methionine salvage; IEA:Ensembl.
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..406
FT /note="Betaine--homocysteine S-methyltransferase 1"
FT /id="PRO_0000234128"
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"
SQ SEQUENCE 406 AA; 45112 MW; 6BCCB007E7ED5B8B CRC64;
MPPVVGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH
REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQKVN EAACDIARQV ADEGDALVAG
GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP
VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL
KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN MGIRYIGGCC
GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSALDMHTK PWVRARARKE YWENLRIASG
RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKLQ
