A0A8X6FYP0 · A0A8X6FYP0_SALDU
- ProteinAconitate hydratase B
- GeneacnB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids865 (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 | 191 | substrate | ||||
Sequence: R | ||||||
Binding site | 244-246 | substrate | ||||
Sequence: SSR | ||||||
Binding site | 414-416 | substrate | ||||
Sequence: QDT | ||||||
Binding site | 498 | substrate | ||||
Sequence: S | ||||||
Binding site | 710 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 769 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 772 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 791 | substrate | ||||
Sequence: R | ||||||
Binding site | 796 | 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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A8X6FYP0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-156 | Aconitase B HEAT-like | ||||
Sequence: EYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPLVSPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWF | ||||||
Domain | 168-382 | Aconitase B swivel | ||||
Sequence: VTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEPDQPGVVGPIKQIEALQKKGYPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGF | ||||||
Domain | 472-818 | Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha | ||||
Sequence: LRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIIEYLTSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAAGKLLDSHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIG |
Sequence similarities
Belongs to the aconitase/IPM isomerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length865
- Mass (Da)93,516
- Last updated2022-12-14 v1
- ChecksumD531EAA34E9C3C1D