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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)DescriptionActionsGraphical viewLength
Metal bindingi217Zinc1
Metal bindingi299Zinc1
Metal bindingi300Zinc1

GO - Molecular functioni

  • betaine-homocysteine S-methyltransferase activity Source: RGD
  • methyltransferase activity Source: RGD
  • protein complex binding Source: RGD
  • S-adenosylmethionine-homocysteine S-methyltransferase activity Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001146242 – 407Betaine--homocysteine S-methyltransferase 1Add BLAST406

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-succinyllysineBy similarity1
Modified residuei93N6-succinyllysineBy similarity1
Modified residuei98N6-succinyllysineBy similarity1
Modified residuei232N6-succinyllysineBy similarity1
Modified residuei241N6-succinyllysineBy similarity1
Modified residuei330PhosphoserineCombined sources1
Modified residuei340N6-succinyllysineBy similarity1
Modified residuei377N6-succinyllysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO09171.
PRIDEiO09171.

PTM databases

iPTMnetiO09171.
PhosphoSitePlusiO09171.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011200.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiO09171. 2 interactors.
STRINGi10116.ENSRNOP00000015336.

Structurei

Secondary structure

1407
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 18Combined sources6
Helixi29 – 35Combined sources7
Turni41 – 43Combined sources3
Helixi48 – 51Combined sources4
Helixi53 – 66Combined sources14
Beta strandi70 – 72Combined sources3
Helixi96 – 112Combined sources17
Turni113 – 115Combined sources3
Beta strandi117 – 122Combined sources6
Helixi126 – 129Combined sources4
Helixi134 – 150Combined sources17
Beta strandi154 – 158Combined sources5
Helixi164 – 175Combined sources12
Beta strandi181 – 185Combined sources5
Helixi198 – 207Combined sources10
Beta strandi211 – 219Combined sources9
Helixi221 – 236Combined sources16
Turni237 – 239Combined sources3
Beta strandi243 – 247Combined sources5
Helixi261 – 263Combined sources3
Turni265 – 269Combined sources5
Helixi272 – 274Combined sources3
Helixi278 – 291Combined sources14
Helixi304 – 313Combined sources10
Helixi315 – 318Combined sources4
Helixi323 – 327Combined sources5
Beta strandi330 – 332Combined sources3
Helixi333 – 335Combined sources3
Helixi341 – 344Combined sources4
Helixi349 – 354Combined sources6
Helixi378 – 397Combined sources20

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO09171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 314Hcy-bindingPROSITE-ProRule annotationAdd BLAST304

Sequence similaritiesi

Contains 1 Hcy-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
HOGENOMiHOG000231636.
HOVERGENiHBG080367.
InParanoidiO09171.
KOiK00544.
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)DescriptionActionsGraphical viewLength
Sequence conflicti247 – 248HA → QP in AAH78811 (PubMed:15489334).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UMYX-ray2.50A/B/C/D1-407[»]
ProteinModelPortaliO09171.
SMRiO09171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO09171. 2 interactors.
STRINGi10116.ENSRNOP00000015336.

PTM databases

iPTMnetiO09171.
PhosphoSitePlusiO09171.

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.
PhylomeDBiO09171.
TreeFamiTF329202.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO09171.
PROiO09171.

Gene expression databases

BgeeiENSRNOG00000011200.

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...

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: November 2, 2016
This is version 132 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.