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Protein

S-methylmethionine--homocysteine S-methyltransferase BHMT2

Gene

Bhmt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor.1 Publication

Catalytic activityi

S-methyl-L-methionine + L-homocysteine = 2 L-methionine.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (BhmT route).
Proteins known to be involved in this subpathway in this organism are:
  1. Betaine--homocysteine S-methyltransferase 1 (Bhmt), S-methylmethionine--homocysteine S-methyltransferase BHMT2 (Bhmt2)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (BhmT route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi208 – 2081ZincPROSITE-ProRule annotation
Metal bindingi290 – 2901ZincPROSITE-ProRule annotation
Metal bindingi291 – 2911ZincPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00051; UER00083.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methylmethionine--homocysteine S-methyltransferase BHMT2 (EC:2.1.1.10)
Short name:
SMM-hcy methyltransferase
Alternative name(s):
Betaine--homocysteine S-methyltransferase 2
Gene namesi
Name:Bhmt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1891379. Bhmt2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363S-methylmethionine--homocysteine S-methyltransferase BHMT2PRO_0000273225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei321 – 3211Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ91WS4.
PRIDEiQ91WS4.

PTM databases

PhosphoSiteiQ91WS4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ91WS4.
CleanExiMM_BHMT2.
GenevisibleiQ91WS4. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015941.

Structurei

3D structure databases

ProteinModelPortaliQ91WS4.
SMRiQ91WS4. Positions 10-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 305295Hcy-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Hcy-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0646.
GeneTreeiENSGT00390000003122.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiQ91WS4.
OMAiPEGDMHD.
OrthoDBiEOG79GT7C.
PhylomeDBiQ91WS4.
TreeFamiTF329202.

Family and domain databases

Gene3Di3.20.20.330. 1 hit.
InterProiIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF037505. Betaine_HMT. 1 hit.
SUPFAMiSSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91WS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPAGSTRAK KGILERLDSG EVVVGDSGFL FTLEKRGFVK AGLWTPEAVV
60 70 80 90 100
EHPSAVRQLH TEFLRAGADV LQTFTFSATE DNMASKWEAV NAAACDLAQE
110 120 130 140 150
VAGGGGALVA GGICQTSLYK YHKDETRIKN IFRLQLEVFA RKNVDFLIAE
160 170 180 190 200
YFEHVEEAVW AVEVLREVGA PVAVTMCIGP EGDMHDVTPG ECAVKLARAG
210 220 230 240 250
ADIIGVNCRF GPWTSLQTMK LMKEGLRDAS LQAHLMVQCL GFHTPDCGKG
260 270 280 290 300
GFVDLPEYPF GLEPRVATRW DIQKYAREAY NLGIRYIGGC CGFEPYHIRA
310 320 330 340 350
IAEELAPERG FLPPASEKHG SWGSGLNMHT KPWIRARARR EYWENLLPAS
360
GRPFCPSLSK PDA
Length:363
Mass (Da):39,872
Last modified:January 23, 2007 - v2
Checksum:iC7367F1B10B07EEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131I → V in AAG41357 (PubMed:11087663).Curated
Sequence conflicti27 – 271S → G in AAH13515 (PubMed:15489334).Curated
Sequence conflicti36 – 361R → G in AAG41357 (PubMed:11087663).Curated
Sequence conflicti327 – 3271N → S in AAG41357 (PubMed:11087663).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26689.1.
RefSeqiNP_075022.2. NM_022884.2.
UniGeneiMm.29981.

Genome annotation databases

EnsembliENSMUST00000015941; ENSMUSP00000015941; ENSMUSG00000042118.
GeneIDi64918.
KEGGimmu:64918.
UCSCiuc007rlk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS26689.1.
RefSeqiNP_075022.2. NM_022884.2.
UniGeneiMm.29981.

3D structure databases

ProteinModelPortaliQ91WS4.
SMRiQ91WS4. Positions 10-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000015941.

PTM databases

PhosphoSiteiQ91WS4.

Proteomic databases

PaxDbiQ91WS4.
PRIDEiQ91WS4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015941; ENSMUSP00000015941; ENSMUSG00000042118.
GeneIDi64918.
KEGGimmu:64918.
UCSCiuc007rlk.1. mouse.

Organism-specific databases

CTDi23743.
MGIiMGI:1891379. Bhmt2.

Phylogenomic databases

eggNOGiCOG0646.
GeneTreeiENSGT00390000003122.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiQ91WS4.
OMAiPEGDMHD.
OrthoDBiEOG79GT7C.
PhylomeDBiQ91WS4.
TreeFamiTF329202.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00083.

Miscellaneous databases

NextBioi320219.
PROiQ91WS4.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WS4.
CleanExiMM_BHMT2.
GenevisibleiQ91WS4. MM.

Family and domain databases

Gene3Di3.20.20.330. 1 hit.
InterProiIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF037505. Betaine_HMT. 1 hit.
SUPFAMiSSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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.

Entry informationi

Entry nameiBHMT2_MOUSE
AccessioniPrimary (citable) accession number: Q91WS4
Secondary accession number(s): B1B1C9, Q8C1U2, Q9EQE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.