Reviewed,
UniProtKB/Swiss-Prot P0A1P8 (GLRX1_SALTY)
Last modified
June 16, 2009.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutaredoxin-1 Short name=Grx1 | ||||
| Gene names |
| ||||
| Organism | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 87 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase By similarity. |
| Subunit structure | Monomer By similarity. |
| Sequence similarities | Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Deoxyribonucleotide synthesis Electron transport Transport |
| Domain | Redox-active center |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activityInferred 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 – 87 | 87 | Glutaredoxin-1 | PRO_0000141583 | |||||||
Regions | |||||||||||
| Domain | 1 – 87 | 87 | Glutaredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 11 ↔ 14 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 50 – 53 | 4 | KTVG → QNRS in AAD18026. Ref.1 | ||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of the major nitrotreductase from Salmonella typhimurium TA1535." Lambert I.B., Boroumandi S., Nokhbeh M.R., Pokorny N.S., Koziarz P. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29629 / TA 1535. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
Cross-references
Sequence databases | |
|---|---|
| AF117952 Genomic DNA. Translation: AAD18026.1. AE008736 Genomic DNA. Translation: AAL19808.1. | |
| RefSeq | NP_459849.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EGO based on UniProtKB P00277. |
| SMR | P0A1P8. Positions 1-84. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1252391. |
| GenomeReviews | Gene locus STM0872 in contig AE006468_GR. |
| KEGG | stm:STM0872. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A1P8. |
| OMA | P0A1P8. KYVDIHA. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM0872-MON. |
Family and domain databases | |
| InterPro | IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR011902. GRXA. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00462. Glutaredoxin. 1 hit. [Graphical view] |
| PRINTS | PR00160. GLUTAREDOXIN. |
| TIGRFAMs | TIGR02183. GRXA. 1 hit. |
| PROSITE | PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLRX1_SALTY | ||||||||
| Accession | Primary (citable) accession number: P0A1P8 Secondary accession number(s): Q9Z5Z3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


