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Protein

Betaine--homocysteine S-methyltransferase 1

Gene

Bhmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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+Note: Binds 1 zinc ion per subunit.

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. S-methylmethionine--homocysteine S-methyltransferase BHMT2 (Bhmt2), Betaine--homocysteine S-methyltransferase 1 (Bhmt), 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 – 2171Zinc
Metal bindingi299 – 2991Zinc
Metal bindingi300 – 3001Zinc

GO - Molecular functioni

  • betaine-homocysteine S-methyltransferase activity Source: RGD
  • methyltransferase activity Source: RGD
  • protein complex binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • amino-acid betaine catabolic process Source: UniProtKB-UniPathway
  • methionine biosynthetic process Source: RGD
  • protein methylation Source: RGD
  • response to organonitrogen compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9241.
BRENDAi2.1.1.5. 5301.
UniPathwayiUPA00051; UER00083.
UPA00291; UER00432.

Names & Taxonomyi

Protein namesi
Recommended name:
Betaine--homocysteine S-methyltransferase 1 (EC:2.1.1.5)
Gene namesi
Name:Bhmt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621496. Bhmt.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • protein complex Source: RGD
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_0000114624Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO09171.
PRIDEiO09171.

PTM databases

iPTMnetiO09171.
PhosphoSiteiO09171.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiO09171. 2 interactions.
STRINGi10116.ENSRNOP00000015336.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 186Combined sources
Helixi29 – 357Combined sources
Turni41 – 433Combined sources
Helixi48 – 514Combined sources
Helixi53 – 6614Combined sources
Beta strandi70 – 723Combined sources
Helixi96 – 11217Combined sources
Turni113 – 1153Combined sources
Beta strandi117 – 1226Combined sources
Helixi126 – 1294Combined sources
Helixi134 – 15017Combined sources
Beta strandi154 – 1585Combined sources
Helixi164 – 17512Combined sources
Beta strandi181 – 1855Combined sources
Helixi198 – 20710Combined sources
Beta strandi211 – 2199Combined sources
Helixi221 – 23616Combined sources
Turni237 – 2393Combined sources
Beta strandi243 – 2475Combined sources
Helixi261 – 2633Combined sources
Turni265 – 2695Combined sources
Helixi272 – 2743Combined sources
Helixi278 – 29114Combined sources
Helixi304 – 31310Combined sources
Helixi315 – 3184Combined sources
Helixi323 – 3275Combined sources
Beta strandi330 – 3323Combined sources
Helixi333 – 3353Combined sources
Helixi341 – 3444Combined sources
Helixi349 – 3546Combined sources
Helixi378 – 39720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UMYX-ray2.50A/B/C/D1-407[»]
ProteinModelPortaliO09171.
SMRiO09171. Positions 10-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09171.

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.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiO09171.
KOiK00544.
OrthoDBiEOG79GT7C.
PhylomeDBiO09171.
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.

O09171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPIAGKKAK RGILERLNAG EVVIGDGGFV FALEKRGYVK AGPWTPEAAV
60 70 80 90 100
EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV AEKISGQKVN
110 120 130 140 150
EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKI FHQQLEVFMK
160 170 180 190 200
KNVDFLIAEY FEHVEEAVWA VEALKTSGKP IAATMCIGPE GDLHGVSPGE
210 220 230 240 250
CAVRLVKAGA AIVGVNCHFD PSTSLQTIKL MKEGLEAARL KAYLMSHALA
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 RPYNPSMSKP DAWGVTKGAA ELMQQKEATT EQQLRALFEK

QKFKSAQ
Length:407
Mass (Da):44,976
Last modified:July 1, 1997 - v1
Checksum:i36E1D04A8E425887
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2482HA → QP in AAH78811 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96133 mRNA. Translation: AAB53763.1.
AF038870 mRNA. Translation: AAB95481.1.
BC078811 mRNA. Translation: AAH78811.1.
RefSeqiNP_110477.1. NM_030850.1.
UniGeneiRn.11406.

Genome annotation databases

GeneIDi81508.
KEGGirno:81508.
UCSCiRGD:621496. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96133 mRNA. Translation: AAB53763.1.
AF038870 mRNA. Translation: AAB95481.1.
BC078811 mRNA. Translation: AAH78811.1.
RefSeqiNP_110477.1. NM_030850.1.
UniGeneiRn.11406.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UMYX-ray2.50A/B/C/D1-407[»]
ProteinModelPortaliO09171.
SMRiO09171. Positions 10-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO09171. 2 interactions.
STRINGi10116.ENSRNOP00000015336.

PTM databases

iPTMnetiO09171.
PhosphoSiteiO09171.

Proteomic databases

PaxDbiO09171.
PRIDEiO09171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81508.
KEGGirno:81508.
UCSCiRGD:621496. rat.

Organism-specific databases

CTDi635.
RGDi621496. Bhmt.

Phylogenomic databases

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiO09171.
KOiK00544.
OrthoDBiEOG79GT7C.
PhylomeDBiO09171.
TreeFamiTF329202.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00083.
UPA00291; UER00432.
BioCyciMetaCyc:MONOMER-9241.
BRENDAi2.1.1.5. 5301.

Miscellaneous databases

EvolutionaryTraceiO09171.
NextBioi614975.
PROiO09171.

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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiBHMT1_RAT
AccessioniPrimary (citable) accession number: O09171
Secondary accession number(s): Q6AZ06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: May 11, 2016
This is version 127 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.