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Protein

Betaine--homocysteine S-methyltransferase 1

Gene

Bhmt

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 betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.

Catalytic activityi

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

Cofactori

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

Pathwayi: betaine degradation

This protein is involved in step 1 of the subpathway that synthesizes sarcosine from betaine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Betaine--homocysteine S-methyltransferase 1 (Bhmt)
  2. Dimethylglycine dehydrogenase, mitochondrial (Dmgdh)
This subpathway is part of the pathway betaine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sarcosine from betaine, the pathway betaine degradation and in Amine and polyamine degradation.

Pathwayi: 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 bindingi217 – 2171ZincPROSITE-ProRule annotation
Metal bindingi299 – 2991ZincPROSITE-ProRule annotation
Metal bindingi300 – 3001ZincPROSITE-ProRule annotation

GO - Molecular functioni

  • betaine-homocysteine S-methyltransferase activity Source: MGI
  • zinc ion binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.5. 3474.
ReactomeiR-MMU-1614635. Sulfur amino acid metabolism.
UniPathwayiUPA00051; UER00083.
UPA00291; UER00432.

Names & Taxonomyi

Protein namesi
Recommended name:
Betaine--homocysteine S-methyltransferase 1 (EC:2.1.1.5)
Gene namesi
Name:Bhmt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 13, Chromosome 18

Organism-specific databases

MGIiMGI:1339972. Bhmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 407406Betaine--homocysteine S-methyltransferase 1PRO_0000114622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-succinyllysineCombined sources
Modified residuei93 – 931N6-succinyllysineCombined sources
Modified residuei98 – 981N6-succinyllysineCombined sources
Modified residuei232 – 2321N6-succinyllysineCombined sources
Modified residuei241 – 2411N6-succinyllysineCombined sources
Modified residuei330 – 3301PhosphoserineBy similarity
Modified residuei340 – 3401N6-succinyllysineCombined sources
Modified residuei377 – 3771N6-succinyllysineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35490.
MaxQBiO35490.
PaxDbiO35490.
PRIDEiO35490.

2D gel databases

REPRODUCTION-2DPAGEO35490.

PTM databases

iPTMnetiO35490.
PhosphoSiteiO35490.
SwissPalmiO35490.

Expressioni

Gene expression databases

BgeeiO35490.
CleanExiMM_BHMT.
GenevisibleiO35490. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiO35490. 3 interactions.
MINTiMINT-1870182.
STRINGi10090.ENSMUSP00000135956.

Structurei

3D structure databases

ProteinModelPortaliO35490.
SMRiO35490. Positions 10-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 314304Hcy-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Hcy-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
GeneTreeiENSGT00390000003122.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiO35490.
KOiK00544.
OMAiAQPLAYH.
OrthoDBiEOG79GT7C.
PhylomeDBiO35490.
TreeFamiTF329202.

Family and domain databases

Gene3Di3.20.20.330. 1 hit.
InterProiIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. HCY_dom.
[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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVAGKKAK KGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV
60 70 80 90 100
EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN
110 120 130 140 150
EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSEVEVKKI FRQQLEVFMK
160 170 180 190 200
KNVDFLIAEY FEHVEEAVWA VEALKASGKP VAATMCIGPE GDLHGVPPGE
210 220 230 240 250
CAVRLVKAGA SIVGVNCHFD PSVSLQTVKL MKEGLEAARL KAYLMSQPLA
260 270 280 290 300
YHTPDCGKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC
310 320 330 340 350
GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWIRARARKE
360 370 380 390 400
YWQNLRIASG RPYNPSMSRP DAWGVTKGAA ELMQQKEATT EQQLRELFEK

QKFKSAQ
Length:407
Mass (Da):45,021
Last modified:January 1, 1998 - v1
Checksum:i1C600BE9CC44EE32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71K → E in BAE26578 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AH009623 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.
CCDSiCCDS36748.1.
RefSeqiNP_057877.1. NM_016668.3.
UniGeneiMm.329582.
Mm.423099.

Genome annotation databases

EnsembliENSMUST00000091776; ENSMUSP00000135956; ENSMUSG00000069324.
ENSMUST00000099309; ENSMUSP00000096912; ENSMUSG00000074768.
GeneIDi12116.
KEGGimmu:12116.
UCSCiuc007rli.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AH009623 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.
CCDSiCCDS36748.1.
RefSeqiNP_057877.1. NM_016668.3.
UniGeneiMm.329582.
Mm.423099.

3D structure databases

ProteinModelPortaliO35490.
SMRiO35490. Positions 10-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35490. 3 interactions.
MINTiMINT-1870182.
STRINGi10090.ENSMUSP00000135956.

PTM databases

iPTMnetiO35490.
PhosphoSiteiO35490.
SwissPalmiO35490.

2D gel databases

REPRODUCTION-2DPAGEO35490.

Proteomic databases

EPDiO35490.
MaxQBiO35490.
PaxDbiO35490.
PRIDEiO35490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091776; ENSMUSP00000135956; ENSMUSG00000069324.
ENSMUST00000099309; ENSMUSP00000096912; ENSMUSG00000074768.
GeneIDi12116.
KEGGimmu:12116.
UCSCiuc007rli.1. mouse.

Organism-specific databases

CTDi635.
MGIiMGI:1339972. Bhmt.

Phylogenomic databases

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
GeneTreeiENSGT00390000003122.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiO35490.
KOiK00544.
OMAiAQPLAYH.
OrthoDBiEOG79GT7C.
PhylomeDBiO35490.
TreeFamiTF329202.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00083.
UPA00291; UER00432.
BRENDAi2.1.1.5. 3474.
ReactomeiR-MMU-1614635. Sulfur amino acid metabolism.

Miscellaneous databases

NextBioi280431.
PROiO35490.
SOURCEiSearch...

Gene expression databases

BgeeiO35490.
CleanExiMM_BHMT.
GenevisibleiO35490. MM.

Family and domain databases

Gene3Di3.20.20.330. 1 hit.
InterProiIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. HCY_dom.
[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. "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] [Europe PMC] [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] [Europe PMC] [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.
    , 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.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-93; LYS-98; LYS-232; LYS-241; LYS-340 AND LYS-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBHMT1_MOUSE
AccessioniPrimary (citable) accession number: O35490
Secondary accession number(s): Q3UEM1, Q3UL72, Q561N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 128 of the entry and version 1 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

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 one 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.