Q8UJ99 (SAHH_AGRT5) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 70.
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 |
| ||||||
| Organism | Agrobacterium tumefaciens (strain C58 / ATCC 33970) | ||||||
| Taxonomic identifier | 176299 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium |
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 Reference 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_0000116939 | |||||
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
| ||||||||||||||||||
References
| [1] | "The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. Nester E.W.Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970. |
| [2] | "Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. Slater S.Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE007869 Genomic DNA. Translation: AAK85853.1. |
| PIR | AF2580. D97362. |
| RefSeq | NP_353068.1. NC_003062.2. |
3D structure databases | |
| ProteinModelPortal | Q8UJ99. |
| SMR | Q8UJ99. Positions 5-466. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8UJ99. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1132067. |
| GenomeReviews | Gene locus Atu0029 in contig AE007869_GR. |
| KEGG | atu:Atu0029. |
| PATRIC | 20809746. VBIAgrTum91616_0029. |
Phylogenomic databases | |
| eggNOG | COG0499. |
| HOGENOM | HBG352029. |
| OMA | SAQVWVT. |
| PhylomeDB | Q8UJ99. |
| ProtClustDB | PRK05476. |
Enzyme and pathway databases | |
| BioCyc | ATUM176299-1:ATU0029-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_AGRT5 | ||||||||
| Accession | Primary (citable) accession number: Q8UJ99 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with