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Q91WS4 (BHMT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. 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:
S-methylmethionine--homocysteine S-methyltransferase BHMT2
Short name=SMM-hcy methyltransferase
EC=2.1.1.5
Alternative name(s):
Betaine--homocysteine S-methyltransferase 2
Gene names
Name:Bhmt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Ref.5

Catalytic activity

Trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine. Ref.5

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.

Tissue specificity

Expressed in fetal heart, lung, liver, kidney and eye. Ref.1

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363S-methylmethionine--homocysteine S-methyltransferase BHMT2
PRO_0000273225

Regions

Domain11 – 305295Hcy-binding

Sites

Metal binding2081Zinc By similarity
Metal binding2901Zinc By similarity
Metal binding2911Zinc By similarity

Experimental info

Sequence conflict131I → V in AAG41357. Ref.1
Sequence conflict271S → G in AAH13515. Ref.4
Sequence conflict361R → G in AAG41357. Ref.1
Sequence conflict3271N → S in AAG41357. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91WS4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C7367F1B10B07EEF

FASTA36339,872
        10         20         30         40         50         60 
MAPAGSTRAK KGILERLDSG EVVVGDSGFL FTLEKRGFVK AGLWTPEAVV EHPSAVRQLH 

        70         80         90        100        110        120 
TEFLRAGADV LQTFTFSATE DNMASKWEAV NAAACDLAQE VAGGGGALVA GGICQTSLYK 

       130        140        150        160        170        180 
YHKDETRIKN IFRLQLEVFA RKNVDFLIAE YFEHVEEAVW AVEVLREVGA PVAVTMCIGP 

       190        200        210        220        230        240 
EGDMHDVTPG ECAVKLARAG ADIIGVNCRF GPWTSLQTMK LMKEGLRDAS LQAHLMVQCL 

       250        260        270        280        290        300 
GFHTPDCGKG GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGIRYIGGC CGFEPYHIRA 

       310        320        330        340        350        360 
IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS GRPFCPSLSK 


PDA

« Hide

References

« Hide 'large scale' references
[1]"Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes."
Chadwick L.H., McCandless S.E., Silverman G.L., Schwartz S., Westaway D., Nadeau J.H.
Genomics 70:66-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Gall bladder and Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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].
Strain: FVB/N.
Tissue: Kidney.
[5]"Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase."
Szegedi S.S., Castro C.C., Koutmos M., Garrow T.A.
J. Biol. Chem. 283:8939-8945(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF257474 mRNA. Translation: AAG41357.1.
AK090308 mRNA. Translation: BAC41163.1.
AK145901 mRNA. Translation: BAE26737.1.
CT030023, AC158524 Genomic DNA. Translation: CAO77969.1.
BC013515 mRNA. Translation: AAH13515.1.
IPIIPI00471239.
RefSeqNP_075022.2. NM_022884.2.
UniGeneMm.29981.

3D structure databases

ProteinModelPortalQ91WS4.
SMRQ91WS4. Positions 10-363.
ModBaseSearch...

PTM databases

PhosphoSiteQ91WS4.

Proteomic databases

PaxDbQ91WS4.
PRIDEQ91WS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015941; ENSMUSP00000015941; ENSMUSG00000042118.
GeneID64918.
KEGGmmu:64918.
UCSCuc007rlk.1. mouse.

Organism-specific databases

CTD23743.
MGIMGI:1891379. Bhmt2.

Phylogenomic databases

eggNOGCOG0646.
GeneTreeENSGT00390000003122.
HOGENOMHOG000231636.
HOVERGENHBG080367.
InParanoidB1B1C9.
OMAGFHTPDC.
OrthoDBEOG4001JM.

Enzyme and pathway databases

UniPathwayUPA00051; UER00083.
UPA00291; UER00432.

Gene expression databases

BgeeQ91WS4.
CleanExMM_BHMT2.
GenevestigatorQ91WS4.

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

NextBio320219.
SOURCESearch...

Entry information

Entry nameBHMT2_MOUSE
AccessionPrimary (citable) accession number: Q91WS4
Secondary accession number(s): B1B1C9, Q8C1U2, Q9EQE8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 74 of the entry and version 2 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