Q9S1H0 (SERA_THASE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 67.
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: Selenate reductase subunit alpha EC=1.97.1.9 Alternative name(s): Selenate reductase molybdenum subunit | ||
| Gene names |
| ||
| Organism | Thauera selenatis | ||
| Taxonomic identifier | 33058 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera![]() |
Protein attributes
| Sequence length | 918 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Terminal reductase that allows anaerobic growth on selenate as the sole respiratory oxidant. |
| Catalytic activity | Selenite + H2O + acceptor = selenate + reduced acceptor. |
| Cofactor | Binds 1 4Fe-4S cluster Potential. Molybdenum (molybdopterin). |
| Enzyme regulation | Inhibited by O2. |
| Subunit structure | Heterotrimer of alpha, beta and gamma subunits. |
| Subcellular location | |
| Post-translational modification | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. |
| Biotechnological use | Has potential use in bioremediation of waste sites contaminated with selenate, such as agricultural drainage waters. |
| Sequence similarities | Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular_component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion bindingInferred from electronic annotation. Source: InterPro selenate reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 36 | 36 | Tat-type signal Ref.2 | ||||||
| Chain | 37 – 918 | 882 | Selenate reductase subunit alpha | PRO_0000019175 | |||||
Sites | |||||||||
| Metal binding | 73 | 1 | Iron-sulfur (4Fe-4S); via pros nitrogen By similarity | ||||||
| Metal binding | 77 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 81 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 115 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis." Krafft T., Bowen A., Theis F., Macy J.M. DNA Seq. 10:365-377(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Purification and characterization of the selenate reductase from Thauera selenatis." Schroeder I., Rech S., Krafft T., Macy J.M. J. Biol. Chem. 272:23765-23768(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-51, CHARACTERIZATION. |
| [3] | "Crystallization and preliminary X-ray analysis of the selenate reductase from Thauera selenatis." Maher M.J., Macy J.M. Acta Crystallogr. D 58:706-708(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ007744 Genomic DNA. Translation: CAB53372.1. |
3D structure databases | |
| ProteinModelPortal | Q9S1H0. |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 5.A.3.8.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 2.40.40.20. 1 hit. |
| InterPro | IPR009010. Asp_de-COase-like_dom. IPR017840. DMSO_Rdtase_II_Mopterin_su. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006311. TAT_signal. [Graphical view] |
| Pfam | PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view] |
| SUPFAM | SSF50692. Asp_decarb_fold. 1 hit. |
| TIGRFAMs | TIGR03479. DMSO_red_II_alp. 1 hit. |
| PROSITE | PS00551. MOLYBDOPTERIN_PROK_1. False negative. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. False negative. PS51318. TAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERA_THASE | ||||||||
| Accession | Primary (citable) accession number: Q9S1H0 | ||||||||
| 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 |

Clusters with
