Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q32LQ4 (BHMT1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Betaine--homocysteine S-methyltransferase 1

EC=2.1.1.5
Gene names
Name:bhmt
ORF Names:wu:fb53h01, zgc:123027
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 Hcy-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Betaine--homocysteine S-methyltransferase 1
PRO_0000273221

Regions

Domain8 – 309302Hcy-binding

Sites

Metal binding2121Zinc By similarity
Metal binding2941Zinc By similarity
Metal binding2951Zinc By similarity

Experimental info

Sequence conflict1891H → P in AAV74219. Ref.1
Sequence conflict1921I → T in AAV74219. Ref.1
Sequence conflict2241A → V in AAV74219. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q32LQ4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: A6A3A9A824D5D26A

FASTA40044,066
        10         20         30         40         50         60 
MAPVGSKRGV LERLNAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF 

        70         80         90        100        110        120 
LRAGSNVMQT FTFYASDDKL ENRGNKLSFT GQQINEAACD LAREVANEGD ALVAGGVSQT 

       130        140        150        160        170        180 
PSYLSCKSEE EVKKTFKKQL DVFIKKNVDL LIAEYFEHVE EAEWAVQVLK ATGKPVAATL 

       190        200        210        220        230        240 
CIGPDGDMHG VIPGECAVRL VKAGADIVGV NCHFDPLTCV KTVAMMKAAV EKAGLKAHYM 

       250        260        270        280        290        300 
TQPLAYHTPD CSCQGFIDLP EFPFALEPRI LTRWEMQQYA REAYKAGIRY IGGCCGFEPY 

       310        320        330        340        350        360 
HIRAVAEELS AERGFLPEAS QKHGLWGSGL EMHTKPWVRA RARRDYWEKL KPASGRPLCP 

       370        380        390        400 
SMSTPDGWGV TRGHAALMQQ KEATTAEQLR PLFQQADAKH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular genetic analysis of folate metabolism in the zebrafish."
Lapek J.D. Jr., Warren J.T. Jr.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY830415 mRNA. Translation: AAV74219.1.
BC109472 mRNA. Translation: AAI09473.1.
IPIIPI00491662.
RefSeqNP_001012498.1. NM_001012480.1.
UniGeneDr.75610.

3D structure databases

ProteinModelPortalQ32LQ4.
SMRQ32LQ4. Positions 7-393.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ32LQ4.

Proteomic databases

PRIDEQ32LQ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID322228.
KEGGdre:322228.

Organism-specific databases

CTD635.
ZFINZDB-GENE-030131-947. bhmt.

Phylogenomic databases

eggNOGfiNOG08394.
GeneTreeENSGT00390000003122.
HOGENOMHBG713318.
HOVERGENHBG080367.
OrthoDBEOG4001JM.
PhylomeDBQ32LQ4.

Gene expression databases

ArrayExpressQ32LQ4.
BgeeQ32LQ4.

Family and domain databases

InterProIPR017226. Betaine-hCys_S-MeTrfase_BHMT.
IPR003726. S_MeTrfase.
[Graphical view]
Gene3DG3DSA:3.20.20.330. S_methyl_trans. 1 hit.
KOK00544.
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...

Entry information

Entry nameBHMT1_DANRE
AccessionPrimary (citable) accession number: Q32LQ4
Secondary accession number(s): Q5PSM1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 6, 2005
Last modified: November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families