Q39UD3 · Q39UD3_GEOMG
- ProteinAconitate hydratase B
- GeneacnB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids847 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Organic acid metabolism; propanoate degradation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 190 | substrate | ||||
Sequence: R | ||||||
Binding site | 233-235 | substrate | ||||
Sequence: SSR | ||||||
Binding site | 403-405 | substrate | ||||
Sequence: QDT | ||||||
Binding site | 487 | substrate | ||||
Sequence: S | ||||||
Binding site | 703 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 762 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 765 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 784 | substrate | ||||
Sequence: R | ||||||
Binding site | 789 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 2-methylisocitrate dehydratase activity | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | aconitate hydratase activity | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Biological Process | propionate catabolic process, 2-methylcitrate cycle | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAconitate hydratase B
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfuromonadia > Geobacterales > Geobacteraceae > Geobacter
Accessions
- Primary accessionQ39UD3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-155 | Aconitase B HEAT-like | ||||
Sequence: AYLAHEAERKAQGIPALPLNPEQTADLCNLLQNPPAGKEEFLLNLLKERVSPGVDPAAKVKAAFLAEIVKGTKKSPLVSKVDAIRILGTMIGGYNVGPLVEALKDAELAEEAACALSRMTLVYDGFDQVVELSKSNAAAKKVLESWANAEWF | ||||||
Domain | 167-371 | Aconitase B swivel | ||||
Sequence: VKVFKVEGEINTDDFSPAGDAWSRPDIPLHALAMGKTRFPNRLKDIADWRAAGHQVAFVGDVVGTGSSRKSACNSVLWHMGQDIPAVPNKKTAGVIIGGVIAPIFFNTAQDSGALPLKADVTKMNDGDVITINTAKGEISNDKGEVISTFKISPNTLADEFRAGGRIPLIIGRAITEKARKALGLGDTDVFTKPVNPAPKAGQGY | ||||||
Domain | 461-689 | Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha | ||||
Sequence: LKPGDGVIHSWLNRLLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAGAMGFMPLDMPESVLVRFKGKLNPGITLRDAVNAIPYWAIKQGKLTVPKKNKINIFNGRILEMEGLPDLTVEQAFELTDAAAERSAAAGCIQLSKESVATYLRSNVALMKKMIADGYQDAQTLQNRIDAVNEWLKNPQLLEADKNAVETGAYADVIEIDLAEITEPILACPNDPDDVKLLSD | ||||||
Domain | 690-810 | Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha | ||||
Sequence: VAGTPIQDVFLGSCMTNIGHFRAAAEIWRGLKFNPSVRTWICPPTRMDQKQLKDEAYFSVYSAFGARIEIAGCSLCMGNQARVPDGVNMFSTSTRNFDDRIGDGAKVFLGSAELGAVTATL |
Sequence similarities
Belongs to the aconitase/IPM isomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length847
- Mass (Da)91,141
- Last updated2005-11-22 v1
- Checksum22B62FC749FA30B6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000148 EMBL· GenBank· DDBJ | ABB32141.1 EMBL· GenBank· DDBJ | Genomic DNA |