Reviewed,
UniProtKB/Swiss-Prot Q9Z8M4 (TRXB_CHLPN)
Last modified
June 16, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thioredoxin reductase Short name=TRXR EC=1.8.1.9 | ||||
| Gene names |
| ||||
| Organism | Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83558 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydophila |
Protein attributes
| Sequence length | 311 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| Sequence similarities | Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicalsInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro thioredoxin-disulfide 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 311 | 311 | Thioredoxin reductase | PRO_0000166725 | |||||||
Regions | |||||||||||
| Nucleotide binding | 33 – 43 | 11 | FAD By similarity | ||||||||
| Nucleotide binding | 283 – 292 | 10 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 138 ↔ 141 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029. |
| [2] | "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. Fraser C.M.Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39. |
| [3] | "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138. |
| [4] | "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183. |
Cross-references
Sequence databases | |
|---|---|
| AE001363 Genomic DNA. Translation: AAD18463.1. AE002161 Genomic DNA. Translation: AAF38283.1. BA000008 Genomic DNA. Translation: BAA98524.1. AE017158 Genomic DNA. Translation: AAP98256.1. | |
| PIR | B86530. C72093. |
| RefSeq | NP_224519.1. NP_300373.1. NP_444992.1. NP_876599.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1VDC based on UniProtKB Q39243. |
| ModBase | Search... |
2-D gel databases | |
| PHCI-2DPAGE | Q9Z8M4. |
Genome annotation databases | |
| GeneID | 1467006. 894975. 919090. 963713. |
| GenomeReviews | Gene locus CPn_0314 in contig AE001363_GR. Gene locus CP_0444 in contig AE002161_GR. Gene locus CpB0322 in contig AE009440_GR. Gene locus trxB in contig BA000008_GR. |
| KEGG | cpa:CP0444. cpn:CPn0314. cpt:CpB0322. |
| TIGR | CP_0444. |
Phylogenomic databases | |
| HOGENOM | Q9Z8M4. |
| OMA | Q9Z8M4. WDSAIDE. |
Enzyme and pathway databases | |
| BioCyc | CPNE115711:CP_0444-MON. CPNE115713:CPN0314-MON. CPNE138677:CPJ0314-MON. CPNE182082:CPB0322-MON. |
| BRENDA | 1.8.1.9. 264832. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR005982. Thioredox_Rdtase. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01292. TRX_reduct. 1 hit. |
| PROSITE | PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TRXB_CHLPN | ||||||||
| Accession | Primary (citable) accession number: Q9Z8M4 Secondary accession number(s): Q9JQJ8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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