Reviewed,
UniProtKB/Swiss-Prot Q3MHL4 (SAHH_BOVIN)
Last modified
February 9, 2010.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenosylhomocysteinase Short name=AdoHcyase EC=3.3.1.1 Alternative name(s): S-adenosyl-L-homocysteine hydrolase | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 432 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine By similarity. |
| Catalytic activity | S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. |
| Cofactor | Binds 1 NAD per subunit By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. Melanosome By similarity. |
| Sequence similarities | Belongs to the adenosylhomocysteinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | One-carbon metabolism |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Hydrolase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | S-adenosylhomocysteine catabolic process Inferred from sequence or structural similarity. Source: AgBase one-carbon metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Inferred from sequence or structural similarity. Source: AgBase melanosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | adenosylhomocysteinase activity Inferred from sequence or structural similarity. Source: AgBase copper ion bindingInferred from sequence or structural similarity. Source: AgBase protein self-associationInferred from sequence or structural similarity. Source: AgBase |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 432 | 431 | Adenosylhomocysteinase | PRO_0000260217 | |||||
Regions | |||||||||
| Region | 183 – 350 | 168 | NAD binding By similarity | ||||||
Sites | |||||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||
| Binding site | 131 | 1 | Substrate By similarity | ||||||
| Binding site | 156 | 1 | Substrate By similarity | ||||||
| Binding site | 186 | 1 | Substrate By similarity | ||||||
| Binding site | 190 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 408 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT030537 mRNA. Translation: ABQ12977.1. BC105194 mRNA. Translation: AAI05195.1. |
| IPI | IPI00714294. |
| RefSeq | NP_001029487.1. |
| UniGene | Bt.12322 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K0U based on UniProtKB P10760. |
| SMR | Q3MHL4. Positions 3-432. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3MHL4. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000024092; ENSBTAP00000024092; ENSBTAG00000018101; Bos taurus. [Genome view] |
| GeneID | 508158. |
| KEGG | bta:508158. |
Organism-specific databases | |
| CTD | 508158. |
Phylogenomic databases | |
| eggNOG | maNOG13409. |
| HOVERGEN | Q3MHL4. |
| InParanoid | Q3MHL4. |
| OMA | VITHDHM. |
| OrthoDB | EOG9KH5F6. |
| PhylomeDB | Q3MHL4. |
Enzyme and pathway databases | |
| BRENDA | 3.3.1.1. 251. |
Family and domain databases | |
| InterPro | IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR016040. NAD(P)-bd_dom. IPR000043. S-Ado-L-homoCys_hydrolase. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view] |
| PANTHER | PTHR23420. Ad_hcy_hydrolase. 1 hit. |
| Pfam | PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view] |
| PIRSF | PIRSF001109. Ad_hcy_hydrolase. 1 hit. |
| TIGRFAMs | TIGR00936. ahcY. 1 hit. |
| PROSITE | PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SAHH_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3MHL4 Secondary accession number(s): A5D9B8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


