Reviewed,
UniProtKB/Swiss-Prot P47348 (TRXB_MYCGE)
Last modified
June 16, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 | Mycoplasma genitalium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2097 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma |
Protein attributes
| Sequence length | 315 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 – 315 | 315 | Thioredoxin reductase | PRO_0000166737 | |||||||
Regions | |||||||||||
| Nucleotide binding | 45 – 52 | 8 | FAD By similarity | ||||||||
| Nucleotide binding | 288 – 297 | 10 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 145 ↔ 148 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 113 – 122 | 10 | VFSKTVIYAT → FLAKLLSMQQ Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. Venter J.C.Science 270:397-403(1995) [PubMed: 7569993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195. |
| [2] | "A survey of the Mycoplasma genitalium genome by using random sequencing." Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III J. Bacteriol. 175:7918-7930(1993) [PubMed: 8253680] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122. Strain: ATCC 33530 / G-37 / NCTC 10195. |
Cross-references
Sequence databases | |
|---|---|
| L43967 Genomic DNA. Translation: AAC71320.1. U02197 Genomic DNA. Translation: AAD12483.1. | |
| PIR | C64211. |
| RefSeq | NP_072764.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TRB based on UniProtKB P09625. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 875416. |
| GenomeReviews | Gene locus MG102 in contig L43967_GR. |
| KEGG | mge:MG_102. |
| TIGR | MG102. |
Phylogenomic databases | |
| HOGENOM | P47348. |
| OMA | P47348. KVTMLVR. |
Enzyme and pathway databases | |
| BioCyc | MGEN243273:MG_102-MON. |
| BRENDA | 1.8.1.9. 110. |
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_MYCGE | ||||||||
| Accession | Primary (citable) accession number: P47348 Secondary accession number(s): Q49316 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Mycoplasma genitalium Mycoplasma genitalium (strain G-37): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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