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Reviewed, UniProtKB/Swiss-Prot O09171 (BHMT1_RAT)

Last modified October 13, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Betaine--homocysteine S-methyltransferase 1
    EC=2.1.1.5
Gene names
Name: Bhmt
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Chain1 – 407407Betaine--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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O09171-1 [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: 8753772] [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: 10417327] [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: 15489334] [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: 15099744] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

U96133 mRNA. Translation: AAB53763.1.
AF038870 mRNA. Translation: AAB95481.1.
BC078811 mRNA. Translation: AAH78811.1.
IPIIPI00332027.
RefSeqNP_110477.1.
UniGeneRn.11406

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UMYX-ray2.50A/B/C/D1-407[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGO09171.

Proteomic databases

PRIDEO09171.

Genome annotation databases

EnsemblENSRNOT00000015336; ENSRNOP00000015336; ENSRNOG00000011200; Rattus norvegicus. [Genome view]
GeneID81508.
KEGGrno:81508.
UCSCNM_030850. rat.

Organism-specific databases

CTD81508.
RGD621496. Bhmt.

Phylogenomic databases

HOVERGENO09171.

Enzyme and pathway databases

BioCycMetaCyc:MON-9241.
BRENDA2.1.1.5. 248.

Gene expression databases

ArrayExpressO09171.
GenevestigatorO09171.
GermOnlineENSRNOG00000011200. Rattus norvegicus.

Family and domain databases

InterProIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
Gene3DG3DSA:3.20.20.330. S_methyl_trans. 1 hit.
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF037505. Betaine_HMT. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents