A5IIY7 (COMB_THEP1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 24.
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: Probable 2-phosphosulfolactate phosphatase EC=3.1.3.71 | ||||
| Gene names |
| ||||
| Organism | Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 390874 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga |
Protein attributes
| Sequence length | 227 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate. HAMAP MF_00490 |
| Cofactor | Magnesium By similarity. HAMAP MF_00490 |
| Sequence similarities | Belongs to the ComB family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | coenzyme M biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | 2-phosphosulfolactate phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 227 | 227 | Probable 2-phosphosulfolactate phosphatase HAMAP MF_00490 | PRO_1000014476 | |||
Sequences
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References
| [1] | "Complete sequence of Thermotoga petrophila RKU-1." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. Richardson P.Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RKU-1 / ATCC BAA-488 / DSM 13995. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000702 Genomic DNA. Translation: ABQ46160.1. |
| RefSeq | YP_001243736.1. NC_009486.1. |
3D structure databases | |
| ProteinModelPortal | A5IIY7. |
| SMR | A5IIY7. Positions 2-225. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5IIY7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5171406. |
| GenomeReviews | Gene locus Tpet_0131 in contig CP000702_GR. |
| KEGG | tpt:Tpet_0131. |
| PATRIC | 23942987. VBIThePet65348_0132. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2045. |
| HOGENOM | HBG633644. |
| OMA | DFICSGY. |
| ProtClustDB | PRK00886. |
Enzyme and pathway databases | |
| BioCyc | TPET390874:TPET_0131-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00490. ComB. [Tree] |
| InterPro | IPR005238. 2-PSlactate_phosphatase. IPR022995. Pase_ComB. [Graphical view] |
| Gene3D | G3DSA:3.90.1560.10. 2-PSlactate_phosphatase. 1 hit. |
| KO | K05979. |
| Pfam | PF04029. 2-ph_phosp. 1 hit. [Graphical view] |
| SUPFAM | SSF142823. SSF142823. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | COMB_THEP1 | ||||||||
| Accession | Primary (citable) accession number: A5IIY7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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