F6A8G7 (F6A8G7_PSEF1) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 15.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: 3-isopropylmalate dehydratase small subunit HAMAP-Rule MF_01031 EC=4.2.1.33 HAMAP-Rule MF_01031 Alternative name(s): Alpha-IPM isomerase HAMAP-Rule MF_01031 Isopropylmalate isomerase HAMAP-Rule MF_01031 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas fulva (strain 12-X) [Complete proteome] [HAMAP] EMBL AEF23038.1 | ||||
| Taxonomic identifier | 743720 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › ![]() |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Catalytic activity | (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Pathway | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Subunit structure | Heterodimer of LeuC and LeuD By similarity. SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Sequence similarities | Belongs to the LeuD family. LeuD type 1 subfamily. HAMAP-Rule MF_01031 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Molecular function | Lyase SAAS SAAS004431 HAMAP-Rule MF_01031 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | 3-isopropylmalate dehydratase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequences
| ||||||||||||||||||
References
| [1] | "Complete sequence of Pseudomonas fulva 12-X." US DOE Joint Genome Institute Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I., Woyke T. Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12-X. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002727 Genomic DNA. Translation: AEF23038.1. |
| RefSeq | YP_004475132.1. NC_015556.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEF23038; AEF23038; Psefu_3074. |
| GeneID | 10657970. |
| KEGG | pfv:Psefu_3074. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K01704. |
| OMA | YQDNSKR. |
Enzyme and pathway databases | |
| BioCyc | PFUL743720:GHQV-3129-MONOMER. |
| UniPathway | UPA00048; UER00071. |
Family and domain databases | |
| Gene3D | 3.20.19.10. 1 hit. |
| HAMAP | MF_01031. LeuD_type1. |
| InterPro | IPR004431. 3-IsopropMal_deHydase_ssu. IPR015937. Acoase/IPM_deHydtase. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view] |
| PANTHER | PTHR11670. PTHR11670. 1 hit. PTHR11670:SF2. PTHR11670:SF2. 1 hit. |
| Pfam | PF00694. Aconitase_C. 1 hit. [Graphical view] |
| SUPFAM | SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. |
| TIGRFAMs | TIGR00171. leuD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | F6A8G7_PSEF1 | ||||||||
| Accession | Primary (citable) accession number: F6A8G7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
