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O35490 (BHMT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

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_0000114622

Regions

Domain11 – 314304Hcy-binding

Sites

Metal binding2171Zinc By similarity
Metal binding2991Zinc By similarity
Metal binding3001Zinc By similarity

Experimental info

Sequence conflict71K → E in BAE26578. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O35490 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1C600BE9CC44EE32

FASTA40745,021
        10         20         30         40         50         60 
MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH 

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

       130        140        150        160        170        180 
GVSQTPSYLS CKSEVEVKKI FRQQLEVFMK KNVDFLIAEY FEHVEEAVWA VEALKASGKP 

       190        200        210        220        230        240 
VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIVGVNCHFD PSVSLQTVKL MKEGLEAARL 

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

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

       370        380        390        400 
RPYNPSMSRP DAWGVTKGAA ELMQQKEATT EQQLRELFEK QKFKSAQ

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a mouse betaine-homocysteine S-methyltransferase gene and pseudogene."
Neece D.J., Griffiths M.A., Garrow T.A.
Gene 250:31-40(2000) [PubMed: 10854776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvEv.
[2]Sowden M.P., Smith H.C.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129.
Tissue: Liver.
[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].
Strain: FVB/N.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF227432 expand/collapse EMBL AC list , AF227426, AF227428, AF227430, AF227431, AF227429, AF227427, AF227425 Genomic DNA. Translation: AAF85944.1.
AF033381 mRNA. Translation: AAB87501.1.
AK145668 mRNA. Translation: BAE26578.1.
AK149457 mRNA. Translation: BAE28890.1.
AK166754 mRNA. Translation: BAE38995.1.
AK166818 mRNA. Translation: BAE39044.1.
BC037004 mRNA. Translation: AAH37004.1.
BC093510 mRNA. Translation: AAH93510.1.
BC110307 mRNA. Translation: AAI10308.1.
IPIIPI00130950.
RefSeqNP_057877.1. NM_016668.3.
UniGeneMm.329582.
Mm.423099.

3D structure databases

ProteinModelPortalO35490.
SMRO35490. Positions 10-398.
ModBaseSearch...

Protein-protein interaction databases

STRINGO35490.

PTM databases

PhosphoSiteO35490.

2D gel databases

REPRODUCTION-2DPAGEO35490.

Proteomic databases

PRIDEO35490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099309; ENSMUSP00000096912; ENSMUSG00000074768.
GeneID12116.
KEGGmmu:12116.
UCSCuc007rli.1. mouse.

Organism-specific databases

CTD635.
MGIMGI:1339972. Bhmt.

Phylogenomic databases

eggNOGroNOG13179.
GeneTreeENSGT00390000003122.
HOGENOMHBG713318.
HOVERGENHBG080367.
InParanoidO35490.
OMAPLAFHTP.
OrthoDBEOG4001JM.
PhylomeDBO35490.

Gene expression databases

BgeeO35490.
CleanExMM_BHMT.
GenevestigatorO35490.
GermOnlineENSMUSG00000069324. Mus musculus.

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.
KOK00544.
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

NextBio280431.
SOURCESearch...

Entry information

Entry nameBHMT1_MOUSE
AccessionPrimary (citable) accession number: O35490
Secondary accession number(s): Q3UEM1, Q3UL72, Q561N0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents