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Q93088 (BHMT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Betaine--homocysteine S-methyltransferase 1

EC=2.1.1.5
Gene names
Name:BHMT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.

Catalytic activity

Trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine.

Cofactor

Binds 1 zinc ion per subunit.

Pathway

Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2.

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1.

Subunit structure

Homotetramer. Ref.6

Subcellular location

Cytoplasm.

Tissue specificity

Found exclusively in liver and kidney. Ref.4

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 406405Betaine--homocysteine S-methyltransferase 1
PRO_0000114621

Regions

Domain11 – 314304Hcy-binding

Sites

Metal binding2171Zinc
Metal binding2991Zinc
Metal binding3001Zinc

Amino acid modifications

Modified residue401N6-succinyllysine By similarity
Modified residue931N6-succinyllysine By similarity
Modified residue2321N6-succinyllysine By similarity
Modified residue2411N6-succinyllysine By similarity
Modified residue3401N6-succinyllysine By similarity
Modified residue3771N6-succinyllysine By similarity

Natural variations

Natural variant1991G → S.
Corresponds to variant rs59866108 [ dbSNP | Ensembl ].
VAR_061345
Natural variant2391R → Q May decrease risk for coronary artery disease. Ref.1 Ref.7
Corresponds to variant rs3733890 [ dbSNP | Ensembl ].
VAR_015886

Secondary structure

............................................................. 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q93088 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 557855B8CEDD0D54

FASTA40644,998
        10         20         30         40         50         60 
MPPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH 

        70         80         90        100        110        120 
REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQEVN EAACDIARQV ADEGDALVAG 

       130        140        150        160        170        180 
GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP 

       190        200        210        220        230        240 
VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL 

       250        260        270        280        290        300 
KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC 

       310        320        330        340        350        360 
GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG 

       370        380        390        400 
RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ 

« Hide

References

« Hide 'large scale' references
[1]"Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase."
Garrow T.A.
J. Biol. Chem. 271:22831-22838(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-239.
Tissue: Liver.
[2]"Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene."
Park E.I., Garrow T.A.
J. Biol. Chem. 274:7816-7824(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene."
Sunden S.L.F., Renduchintala M.S., Park E.I., Miklasz S.D., Garrow T.A.
Arch. Biochem. Biophys. 345:171-174(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Human betaine-homocysteine methyltransferase is a zinc metalloenzyme."
Millian N.S., Garrow T.A.
Arch. Biochem. Biophys. 356:93-98(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ZINC-BINDING.
Tissue: Liver.
[6]"Betaine-homocysteine methyltransferase: zinc in a distorted barrel."
Evans J.C., Huddler D.P., Jiracek J., Castro C., Millian N.S., Garrow T.A., Ludwig M.L.
Structure 10:1159-1171(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), SUBUNIT.
[7]"Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease."
Weisberg I.S., Park E., Ballman K.V., Berger P., Nunn M., Suh D.S., Breksa A.P., Garrow T.A., Rozen R.
Atherosclerosis 167:205-214(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-239.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50929 mRNA. Translation: AAC50668.1.
AF118378 expand/collapse EMBL AC list , AF118371, AF118372, AF118373, AF118374, AF118375, AF118376, AF118377 Genomic DNA. Translation: AAD22043.1.
BC012616 mRNA. Translation: AAH12616.1.
RefSeqNP_001704.2. NM_001713.2.
UniGeneHs.80756.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LT7X-ray2.15A/B3-406[»]
1LT8X-ray2.05A/B3-406[»]
ProteinModelPortalQ93088.
SMRQ93088. Positions 10-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107104. 6 interactions.
IntActQ93088. 5 interactions.
MINTMINT-246738.
STRING9606.ENSP00000274353.

Chemistry

BindingDBQ93088.
ChEMBLCHEMBL4328.
DrugBankDB00134. L-Methionine.

PTM databases

PhosphoSiteQ93088.

Polymorphism databases

DMDM145559446.

Proteomic databases

PaxDbQ93088.
PRIDEQ93088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274353; ENSP00000274353; ENSG00000145692.
GeneID635.
KEGGhsa:635.
UCSCuc003kfu.4. human.

Organism-specific databases

CTD635.
GeneCardsGC05P078443.
HGNCHGNC:1047. BHMT.
HPAHPA038285.
MIM602888. gene.
neXtProtNX_Q93088.
PharmGKBPA25350.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0646.
HOGENOMHOG000231636.
HOVERGENHBG080367.
InParanoidQ93088.
KOK00544.
OMAWGVTKGT.
OrthoDBEOG79GT7C.
PhylomeDBQ93088.
TreeFamTF329202.

Enzyme and pathway databases

BioCycMetaCyc:HS07273-MONOMER.
BRENDA2.1.1.5. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ93088.
UniPathwayUPA00051; UER00083.
UPA00291; UER00432.

Gene expression databases

ArrayExpressQ93088.
BgeeQ93088.
CleanExHS_BHMT.
GenevestigatorQ93088.

Family and domain databases

Gene3D3.20.20.330. 1 hit.
InterProIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF037505. Betaine_HMT. 1 hit.
SUPFAMSSF82282. SSF82282. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ93088.
GenomeRNAi635.
NextBio2568.
PROQ93088.
SOURCESearch...

Entry information

Entry nameBHMT1_HUMAN
AccessionPrimary (citable) accession number: Q93088
Secondary accession number(s): Q9UNI9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM