Reviewed,
UniProtKB/Swiss-Prot Q8NQ98 (ACON_CORGL)
Last modified
February 9, 2010.
Version 55.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Aconitate hydratase EC=4.2.1.3 | ||||
| Gene names |
| ||||
| Organism | Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 939 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Citrate = isocitrate. |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. |
| Pathway | Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. |
| Induction | Repressed by acnR. |
| Sequence similarities | Belongs to the aconitase/IPM isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro aconitate hydratase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 939 | 939 | Aconitate hydratase | PRO_0000076657 | |||||
Sites | |||||||||
| Metal binding | 475 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 541 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 544 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 71 | 1 | D → N in BAA76717. Ref.1 | ||||||
| Sequence conflict | 122 | 1 | M → V in BAA76717. Ref.1 | ||||||
| Sequence conflict | 555 | 1 | I → Y in BAA76717. Ref.1 | ||||||
| Sequence conflict | 745 | 1 | N → Y in BAA76717. Ref.1 | ||||||
| Sequence conflict | 888 | 1 | T → I in BAA76717. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Brevibacterium lactofermentum ATCC 13869 acn gene for aconitase." Nakamura J., Kimura E., Oosumi T., Matsui K., Nakamatsu T. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567. |
| [2] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [3] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB025424 Genomic DNA. Translation: BAA76717.1. BA000036 Genomic DNA. Translation: BAB98933.1. Different initiation. BX927152 Genomic DNA. Translation: CAF21548.1. Different initiation. |
| RefSeq | NP_600755.1. YP_225824.1. |
3D structure databases | |
| ModBase | Search... |
2-D gel databases | |
| World-2DPAGE | 0001:Q8NQ98. |
Genome annotation databases | |
| GeneID | 1019512. 3344469. |
| GenomeReviews | Gene locus Cgl1540 in contig BA000036_GR. |
| KEGG | cgb:cg1737. cgl:NCgl1482. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG289738. |
| OMA | YSKAQGM. |
| PhylomeDB | Q8NQ98. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:CG1737-MONOMER. |
| BRENDA | 4.2.1.3. 812. |
Family and domain databases | |
| InterPro | IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR006249. Aconitase/Fe_reg_prot_2. IPR015934. Aconitase/Fe_reg_prot_2/AcnD. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view] |
| Gene3D | G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit. |
| PANTHER | PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit. |
| Pfam | PF00330. Aconitase. 2 hits. PF00694. Aconitase_C. 1 hit. [Graphical view] |
| PRINTS | PR00415. ACONITASE. |
| TIGRFAMs | TIGR01341. aconitase_1. 1 hit. |
| PROSITE | PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACON_CORGL | ||||||||
| Accession | Primary (citable) accession number: Q8NQ98 Secondary accession number(s): Q6M550, Q9WXJ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


