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O09171 (BHMT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length407 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.4

Subcellular location

Cytoplasm.

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 407406Betaine--homocysteine S-methyltransferase 1
PRO_0000114624

Regions

Domain11 – 314304Hcy-binding

Sites

Metal binding2171Zinc
Metal binding2991Zinc
Metal binding3001Zinc

Experimental info

Sequence conflict247 – 2482HA → QP in AAH78811. Ref.3

Secondary structure

1 ............................................................ 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O09171 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 36E1D04A8E425887

FASTA40744,976
        10         20         30         40         50         60 
MAPIAGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH 

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

       130        140        150        160        170        180 
GVSQTPSYLS CKSETEVKKI FHQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKTSGKP 

       190        200        210        220        230        240 
IAATMCIGPE GDLHGVSPGE CAVRLVKAGA AIVGVNCHFD PSTSLQTIKL MKEGLEAARL 

       250        260        270        280        290        300 
KAYLMSHALA YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC 

       310        320        330        340        350        360 
GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE YWQNLRIASG 

       370        380        390        400 
RPYNPSMSKP DAWGVTKGAA ELMQQKEATT EQQLRALFEK QKFKSAQ

« Hide

References

« Hide 'large scale' references
[1]"Application of mRNA differential display to liver cirrhosis: reduced fetuin expression in biliary cirrhosis in the rat."
Forestier M., Reichen J., Solioz M.
Biochem. Biophys. Res. Commun. 225:377-383(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Apolipoprotein B mRNA and lipoprotein secretion are increased in McArdle RH-7777 cells by expression of betaine-homocysteine S-methyltransferase."
Sowden M.P., Collins H.L., Smith H.C., Garrow T.A., Sparks J.D., Sparks C.E.
Biochem. J. 341:639-645(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]"Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding."
Gonzalez B., Pajares M.A., Martinez-Ripoll M., Blundell T.L., Sanz-Aparicio J.
J. Mol. Biol. 338:771-782(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U96133 mRNA. Translation: AAB53763.1.
AF038870 mRNA. Translation: AAB95481.1.
BC078811 mRNA. Translation: AAH78811.1.
IPIIPI00332027.
RefSeqNP_110477.1. NM_030850.1.
UniGeneRn.11406.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UMYX-ray2.50A/B/C/D1-407[»]
ProteinModelPortalO09171.
SMRO09171. Positions 10-398.
ModBaseSearch...

Protein-protein interaction databases

IntActO09171. 2 interactions.
STRING10116.ENSRNOP00000015336.

PTM databases

PhosphoSiteO09171.

Proteomic databases

PaxDbO09171.
PRIDEO09171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015336; ENSRNOP00000015336; ENSRNOG00000011200.
GeneID81508.
KEGGrno:81508.
UCSCRGD:621496. rat.

Organism-specific databases

CTD635.
RGD621496. Bhmt.

Phylogenomic databases

eggNOGCOG0646.
GeneTreeENSGT00390000003122.
HOGENOMHOG000231636.
HOVERGENHBG080367.
InParanoidO09171.
KOK00544.
OrthoDBEOG4001JM.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-9241.
BRENDA2.1.1.5. 5301.
UniPathwayUPA00051; UER00083.
UPA00291; UER00432.

Gene expression databases

GenevestigatorO09171.
GermOnlineENSRNOG00000011200. Rattus norvegicus.

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. S_methyl_trans. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO09171.
NextBio614975.

Entry information

Entry nameBHMT1_RAT
AccessionPrimary (citable) accession number: O09171
Secondary accession number(s): Q6AZ06
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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