P0A6V5 (GLPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 59.
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: Thiosulfate sulfurtransferase glpE EC=2.8.1.1 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 108 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of glpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. HAMAP MF_01009 |
| Catalytic activity | Thiosulfate + cyanide = sulfite + thiocyanate. HAMAP MF_01009 |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Induction | By infection by filamentous bacteriophages. Expression is positively regulated by cyclic AMP-cAMP receptor protein (cAMP-CRP). Ref.5 Ref.7 |
| Miscellaneous | Incubation of glpE with the cysteine-specific modifying reagent DTNB resulted in a greater-than-90% loss of activity. HAMAP MF_01009 |
| Sequence similarities | Belongs to the glpE family. Contains 1 rhodanese domain. |
| Sequence caution | The sequence AAA23889.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycerol metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from direct assay Ref.6. Source: EcoCyc |
| Molecular function | thiosulfate sulfurtransferase activity Inferred from direct assay Ref.6. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 108 | 108 | Thiosulfate sulfurtransferase glpE HAMAP MF_01009 | PRO_0000200549 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Domain | 17 – 105 | 89 | Rhodanese | |||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 65 | 1 | Cysteine persulfide intermediate Probable | |||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 108 | 1 | A → RNALYCPLLCGISDSNDVDD YLFC Ref.2 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 5 – 7 | 3 | ||||||||||||||||||||||||||||
| Helix | 9 – 17 | 9 | ||||||||||||||||||||||||||||
| Beta strand | 22 – 25 | 4 | ||||||||||||||||||||||||||||
| Helix | 29 – 34 | 6 | ||||||||||||||||||||||||||||
| Helix | 45 – 54 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 61 – 64 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 66 – 69 | 4 | ||||||||||||||||||||||||||||
| Helix | 70 – 81 | 12 | ||||||||||||||||||||||||||||
| Beta strand | 84 – 89 | 6 | ||||||||||||||||||||||||||||
| Helix | 92 – 99 | 8 | ||||||||||||||||||||||||||||
| Helix | 101 – 103 | 3 | ||||||||||||||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain." Zeng G., Ye S., Larson T.J. J. Bacteriol. 178:7080-7089(1996) [PubMed: 8955387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12." Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K. Nucleic Acids Res. 16:7732-7732(1988) [PubMed: 3045764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Regulation of glpD and glpE gene expression by a cyclic AMP-cAMP receptor protein (cAMP-CRP) complex in Escherichia coli." Choi Y.-L., Kawase S., Kawamukai M., Sakai H., Komano T. Biochim. Biophys. Acta 1088:31-35(1991) [PubMed: 1846566] [Abstract] Cited for: INDUCTION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin." Ray W.K., Zeng G., Potters M.B., Mansuri A.M., Larson T.J. J. Bacteriol. 182:2277-2284(2000) [PubMed: 10735872] [Abstract] Cited for: CHARACTERIZATION. Strain: BL21-DE3. |
| [7] | "Biochemical and genetic characterization of pspE and glpE, two single-domain sulfurtransferases of Escherichia coli." Cheng H., Donahue J.L., Battle S.E., Ray W.K., Larson T.J. Open Microbiol. J. 2:18-28(2008) [PubMed: 19088907] [Abstract] Cited for: INDUCTION. Strain: K12 / MG1655 / ATCC 47076. |
| [8] | "Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 A resolution diffraction: a preliminary report." Bordo D., Larson T.J., Donahue J.L., Spallarossa A., Bolognesi M. Acta Crystallogr. D 56:1691-1693(2000) [PubMed: 11092948] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS). Strain: BL21-DE3. |
| [9] | "Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily." Spallarossa A., Donahue J.L., Larson T.J., Bolognesi M., Bordo D. Structure 9:1117-1125(2001) [PubMed: 11709175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS). Strain: BL21-DE3. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M96795 Genomic DNA. Translation: AAC28165.1. X07520 Genomic DNA. Translation: CAA30397.1. M54940 Genomic DNA. Translation: AAA23889.1. Different initiation. U18997 Genomic DNA. Translation: AAA58223.1. U00096 Genomic DNA. Translation: AAC76450.1. AP009048 Genomic DNA. Translation: BAE77867.1. | ||||||||||||||||||
| PIR | BVECGE. D65138. | ||||||||||||||||||
| RefSeq | NP_417883.1. NC_000913.2. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0A6V5. | ||||||||||||||||||
| SMR | P0A6V5. Positions 1-108. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P0A6V5. 2 interactions. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | EBESCT00000002575; EBESCP00000002575; EBESCG00000002101. EBESCT00000017761; EBESCP00000017052; EBESCG00000016817. | ||||||||||||||||||
| GeneID | 947935. | ||||||||||||||||||
| GenomeReviews | Gene locus JW3388 in contig AP009048_GR. Gene locus b3425 in contig U00096_GR. | ||||||||||||||||||
| KEGG | ecj:JW3388. eco:b3425. | ||||||||||||||||||
| PATRIC | 32122286. VBIEscCol129921_3520. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB0390. | ||||||||||||||||||
| EcoGene | EG10395. glpE. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG0607. | ||||||||||||||||||
| GeneTree | EBGT00050000010658. | ||||||||||||||||||
| HOGENOM | HBG743107. | ||||||||||||||||||
| OMA | FSAWHEA. | ||||||||||||||||||
| PhylomeDB | P0A6V5. | ||||||||||||||||||
| ProtClustDB | PRK00162. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:EG10395-MONOMER. MetaCyc:EG10395-MONOMER. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P0A6V5. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_01009. Thiosulf_sulfurtr. [Tree] | ||||||||||||||||||
| InterPro | IPR001763. Rhodanese-like. IPR023695. Thiosulf_sulfurTrfase. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.40.250.10. Rhodanese-like. 1 hit. | ||||||||||||||||||
| KO | K02439. | ||||||||||||||||||
| Pfam | PF00581. Rhodanese. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00450. RHOD. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF52821. Rhodanese-like. 1 hit. | ||||||||||||||||||
| PROSITE | PS50206. RHODANESE_3. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | GLPE_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A6V5 Secondary accession number(s): P09390, Q2M789, Q47235 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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