| General information | | DisProt: | DP00619 | | Name: | Homoaconitase small subunit | | Synonym(s): | HACB_METJA
Homoaconitate hydratase
(R)-homocitrate dehydratase
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | Q58667 | | UniGene: | | | SwissProt: | HACB_METJA | | TrEMBL: | | | NCBI (GI): | 3122344 | | Source organism: | Methanocaldococcus jannaschii | | Sequence length: | 170 | | Percent disordered: | 2% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MIIKGRAHKF GDDVDTDAII PGPYLRTTDP YELASHCMAG IDENFPKKVK EGDVIVAGEN - 60
FGCGSSREQA VIAIKYCGIK AVIAKSFARI FYRNAINVGL IPIIANTDEI KDGDIVEIDL - 120
DKEEIVITNK NKTIKCETPK GLEREILAAG GLVNYLKKRK LIQSKKGVKT
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| Functional narrative |
Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the nonphysiological cis-homo(4)-aconitate with similar efficiency. Can also catalyze the hydration of maleate to (R)-malate. Can not catalyze the hydration of citraconate or cis-aconitate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Flexible loop | | Location: | 26 - 29 | | Length: | 4 | | Region sequence: |
RTTD | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (295 K; pH: 4.6; glycerol cryoprotectant (v/v) 20 %; PEG 200 (w/v) 50 %; protein solution 1 uL; Tris-HCl 0.1 M)
| References:
- Jeyakanthan J, Drevland RM, Gayathri DR, Velmurugan D, Shinkai A, Kuramitsu S, Yokoyama S, Graham DE. "Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit." Biochemistry. 2010; 49(12): 2687-2696. PubMed: 20170198
| Comments:
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| References |
- Jeyakanthan J, Drevland RM, Gayathri DR, Velmurugan D, Shinkai A, Kuramitsu S, Yokoyama S, Graham DE. "Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit." Biochemistry. 2010; 49(12): 2687-2696. PubMed: 20170198
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| Comments |
AV (7-7-2010) PubMed: 20170198
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