O53442 (DESA2_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 74.
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: Putative acyl-[acyl-carrier-protein] desaturase desA2 Short name=DES EC=1.14.19.- Alternative name(s): Putative acyl-ACP desaturase desA2 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium tuberculosis | ||||
| Taxonomic identifier | 1773 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 275 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Could be involved in mycobacterial fatty acid biosynthesis. Ref.3 |
| Cofactor | Iron. |
| Pathway | |
| Subunit structure | Homodimer. Ref.6 |
| Miscellaneous | Was identified as a high-confidence drug target. |
| Sequence similarities | Belongs to the fatty acid desaturase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | Iron Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Isopeptide bond Ubl conjugation |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW growthInferred from mutant phenotype. Source: MTBBASE |
| Cellular component | cytosol Inferred from direct assay. Source: MTBBASE plasma membraneInferred from direct assay. Source: MTBBASE |
| Molecular function | acyl-[acyl-carrier-protein] desaturase activity Inferred from electronic annotation. Source: InterPro protein homodimerization activityInferred from physical interaction Ref.6. Source: MTBBASE transition metal ion bindingInferred 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 – 275 | 275 | Putative acyl-[acyl-carrier-protein] desaturase desA2 | PRO_0000392676 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Metal binding | 107 | 1 | Iron | ||||||||||||||||||||||||||||||||||
| Metal binding | 159 | 1 | Iron | ||||||||||||||||||||||||||||||||||
| Metal binding | 189 | 1 | Iron | ||||||||||||||||||||||||||||||||||
| Metal binding | 192 | 1 | Iron | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Cross-link | 145 | Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) | |||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Helix | 9 – 27 | 19 | |||||||||||||||||||||||||||||||||||
| Helix | 34 – 37 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 56 – 58 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 63 – 77 | 15 | |||||||||||||||||||||||||||||||||||
| Helix | 103 – 120 | 18 | |||||||||||||||||||||||||||||||||||
| Turn | 126 – 130 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 148 – 160 | 13 | |||||||||||||||||||||||||||||||||||
| Helix | 164 – 172 | 9 | |||||||||||||||||||||||||||||||||||
| Turn | 176 – 178 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 182 – 206 | 25 | |||||||||||||||||||||||||||||||||||
| Helix | 208 – 221 | 14 | |||||||||||||||||||||||||||||||||||
| Helix | 233 – 241 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 248 – 260 | 13 | |||||||||||||||||||||||||||||||||||
| Helix | 267 – 272 | 6 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
| [3] | "Unique mechanism of action of the thiourea drug isoxyl on Mycobacterium tuberculosis." Phetsuksiri B., Jackson M., Scherman H., McNeil M., Besra G.S., Baulard A.R., Slayden R.A., DeBarber A.E., Barry C.E. III, Baird M.S., Crick D.C., Brennan P.J. J. Biol. Chem. 278:53123-53130(2003) [PubMed: 14559907] [Abstract] Cited for: FUNCTION AS A DESATURASE. Strain: ATCC 25618 / H37Rv. |
| [4] | "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS]. |
| [5] | "Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis." Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H. PLoS ONE 5:E8589-E8589(2010) [PubMed: 20066036] [Abstract] Cited for: PUPYLATION AT LYS-145, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv. |
| [6] | "X-ray structure of putative acyl-ACP desaturase DesA2 from Mycobacterium tuberculosis H37Rv." Dyer D.H., Lyle K.S., Rayment I., Fox B.G. Protein Sci. 14:1508-1517(2005) [PubMed: 15929999] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE000516 Genomic DNA. Translation: AAK45384.1. BX842575 Genomic DNA. Translation: CAA17210.1. | ||||||||||||
| PIR | D70896. | ||||||||||||
| RefSeq | NP_215610.1. NC_000962.2. NP_335570.1. NC_002755.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O53442. | ||||||||||||
| SMR | O53442. Positions 8-274. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBMYCT00000003982; EBMYCP00000003982; EBMYCG00000003980. EBMYCT00000071227; EBMYCP00000069286; EBMYCG00000071222. | ||||||||||||
| GeneID | 885339. 924977. | ||||||||||||
| GenomeReviews | Gene locus MT1126 in contig AE000516_GR. Gene locus Rv1094 in contig AL123456_GR. | ||||||||||||
| KEGG | mtc:MT1126. mtu:Rv1094. | ||||||||||||
| PATRIC | 18124238. VBIMycTub22151_1239. | ||||||||||||
| TIGR | MT1126. | ||||||||||||
Organism-specific databases | |||||||||||||
| TubercuList | Rv1094. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000016016. | ||||||||||||
| HOGENOM | HBG566522. | ||||||||||||
| OMA | GYRADTY. | ||||||||||||
| ProtClustDB | CLSK790944. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.14.19.2. 3445. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR005067. Fatty_acid_desaturase-2. IPR009078. Ferritin/RR-like. IPR012348. Ribncl_red-rel. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.620.20. Ribncl_red_rel. 1 hit. | ||||||||||||
| KO | K03922. | ||||||||||||
| Pfam | PF03405. FA_desaturase_2. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF000346. Dlt9_acylACP_des. 1 hit. | ||||||||||||
| SUPFAM | SSF47240. Ferritin/RR_like. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | DESA2_MYCTU | ||||||||
| Accession | Primary (citable) accession number: O53442 Secondary accession number(s): Q7D8V3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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