Q8FXZ7 (SAHH_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adenosylhomocysteinase EC=3.3.1.1 Alternative name(s): S-adenosyl-L-homocysteine hydrolase Short name=AdoHcyase | ||||
| Gene names |
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| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine By similarity. HAMAP MF_00563 |
| Catalytic activity | S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine. HAMAP MF_00563 |
| Cofactor | Binds 1 NAD per subunit By similarity. HAMAP MF_00563 |
| Pathway | Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. HAMAP MF_00563 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00563. |
| Sequence similarities | Belongs to the adenosylhomocysteinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | One-carbon metabolism |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | Adenosylhomocysteinase HAMAP MF_00563 | PRO_0000116952 | |||||
Regions | |||||||||
| Nucleotide binding | 193 – 195 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 256 – 261 | 6 | NAD By similarity | ||||||
| Nucleotide binding | 335 – 337 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||
| Binding site | 132 | 1 | Substrate By similarity | ||||||
| Binding site | 192 | 1 | Substrate By similarity | ||||||
| Binding site | 222 | 1 | Substrate By similarity | ||||||
| Binding site | 226 | 1 | Substrate By similarity | ||||||
| Binding site | 227 | 1 | NAD By similarity | ||||||
| Binding site | 279 | 1 | NAD By similarity | ||||||
| Binding site | 314 | 1 | NAD By similarity | ||||||
| Binding site | 380 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014291 Genomic DNA. Translation: AAN30987.1. CP002997 Genomic DNA. Translation: AEM19404.1. |
| RefSeq | NP_699072.1. NC_004310.3. |
3D structure databases | |
| ProteinModelPortal | Q8FXZ7. |
| SMR | Q8FXZ7. Positions 5-466. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1167800. |
| GenomeReviews | Gene locus BR2097 in contig AE014291_GR. |
| KEGG | bms:BR2097. |
| PATRIC | 17792629. VBIBruSui107850_2135. |
| TIGR | BR2097. |
Phylogenomic databases | |
| HOGENOM | HBG352029. |
| OMA | SAQVWVT. |
| PhylomeDB | Q8FXZ7. |
| ProtClustDB | PRK05476. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_2097-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00563. AdoHcyase. [Tree] |
| InterPro | IPR000043. Adenosylhomocysteinase. IPR015878. Ado_hCys_hydrolase_NAD-bd. IPR020082. S-Ado-L-homoCys_hydrolase_CS. [Graphical view] |
| KO | K01251. |
| 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. |
| SMART | SM00996. AdoHcyase. 1 hit. SM00997. AdoHcyase_NAD. 1 hit. [Graphical view] |
| 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_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FXZ7 Secondary accession number(s): G0K945 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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