Aconitase/3-isopropylmalate dehydratase protein [Arabidopsis thaliana (thale cress)] - Gene

Summary

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Official Full Name: Aconitase/3-isopropylmalate dehydratase protein
Primary source: TAIR:AT2G43090
Locus tag: AT2G43090
See related: Araport:AT2G43090
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Arabidopsis thaliana (ecotype: Columbia)
Lineage: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Also known as: IPMI SSU1; isopropylmalate isomerase small subunit 1; MFL8.15
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Genomic context

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Location:: chromosome: 2

Exon count:: 2

Sequence:: Chromosome: 2; NC_003071.7 (17918926..17920496)

Chromosome 2 - NC_003071.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003071.7

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A function of IPMI small subunit1 in both leucine biosynthesis and the first cycle of Met chain elongation, is reported.[IPM1]
Title: The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation.
ACO3 is cytosolic in young seedlings and functions in citrate catabolism consistent.
Title: Selective induction and subcellular distribution of ACONITASE 3 reveal the importance of cytosolic citrate metabolism during lipid mobilization in Arabidopsis.
AtLeuD3 plays an essential role in leucine biosynthesis and female gametophyte development. [LeuD3]
Title: Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

NM_001202808.1

Supported by ESTs:

NM_129870.3

Supported by ESTs:

Gene Ontology Provided by TAIR

Function	Evidence Code	Pubs
enables 3-isopropylmalate dehydratase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in L-leucine biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within L-leucine biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in L-leucine biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within chloroplast organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in gametophyte development	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within glucosinolate biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in chloroplast	HDA more info	PubMed
located_in chloroplast	ISM Inferred from Sequence Model more info
located_in chloroplast stroma	HDA more info	PubMed
located_in chloroplast stroma	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	ISM Inferred from Sequence Model more info
located_in plastid	HDA more info	PubMed
located_in plastid	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Aconitase/3-isopropylmalate dehydratase protein

NP_001189737.1

Aconitase/3-isopropylmalate dehydratase protein; FUNCTIONS IN: hydro-lyase activity, 3-isopropylmalate dehydratase activity; INVOLVED IN: metabolic process; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: 3-isopropylmalate dehydratase, small subunit-like (InterPro:IPR012305), Aconitase-like core (InterPro:IPR015937), Aconitase/3-isopropylmalate dehydratase, swivel (InterPro:IPR015928); BEST Arabidopsis thaliana protein match is: isopropylmalate isomerase 1 (TAIR:AT3G58990.1).

NP_181837.1

Aconitase/3-isopropylmalate dehydratase protein; FUNCTIONS IN: hydro-lyase activity, 3-isopropylmalate dehydratase activity; INVOLVED IN: response to salt stress, metabolic process; LOCATED IN: chloroplast, chloroplast stroma; EXPRESSED IN: 24 plant structures; EXPRESSED DURING: 14 growth stages; CONTAINS InterPro DOMAIN/s: 3-isopropylmalate dehydratase, small subunit-like (InterPro:IPR012305), Aconitase A/isopropylmalate dehydratase small subunit, swivel (InterPro:IPR000573), Aconitase/3-isopropylmalate dehydratase, swivel (InterPro:IPR015928), Aconitase-like core (InterPro:IPR015937); BEST Arabidopsis thaliana protein match is: isopropylmalate isomerase 1 (TAIR:AT3G58990.1); Has 8413 Blast hits to 8412 proteins in 2279 species: Archae - 351; Bacteria - 5415; Metazoa - 18; Fungi - 351; Plants - 71; Viruses - 0; Other Eukaryotes - 2207 (source: NCBI BLink).

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003071.7 Reference assembly

Range

17918926..17920496

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_129870.3 → NP_181837.1 Aconitase/3-isopropylmalate dehydratase protein [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_181837.1

Status: REVIEWED

UniProtKB/Swiss-Prot

Q9ZW85

UniProtKB/TrEMBL

A0A178W1Y9, A0A5S9X6I6

Conserved Domains (1) summary

PLN00072
Location:1 → 249

PLN00072; 3-isopropylmalate isomerase/dehydratase small subunit; Provisional
NM_001202808.1 → NP_001189737.1 Aconitase/3-isopropylmalate dehydratase protein [Arabidopsis thaliana]

See identical proteins and their annotated locations for NP_001189737.1

Status: REVIEWED

UniProtKB/TrEMBL

F4IQ61

Conserved Domains (2) summary

PLN00072
Location:1 → 220

PLN00072; 3-isopropylmalate isomerase/dehydratase small subunit; Provisional

cl00215
Location:71 → 218

Aconitase_swivel; Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme ...