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UniProtKB - Q1MA52 (LEUD_RHIL3)
Protein
3-isopropylmalate dehydratase small subunit
Gene
leuD
Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Status
Functioni
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
UniRule annotationCatalytic activityi
- EC:4.2.1.33UniRule annotation
: L-leucine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.
GO - Molecular functioni
- 3-isopropylmalate dehydratase activity Source: UniProtKB-UniRule
GO - Biological processi
- leucine biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Lyase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis |
Enzyme and pathway databases
UniPathwayi | UPA00048;UER00071 |
Names & Taxonomyi
Protein namesi | Recommended name: 3-isopropylmalate dehydratase small subunitUniRule annotation (EC:4.2.1.33UniRule annotation)Alternative name(s): Alpha-IPM isomeraseUniRule annotation Short name: IPMIUniRule annotation Isopropylmalate isomeraseUniRule annotation |
Gene namesi | Name:leuDUniRule annotation Ordered Locus Names:RL4705 |
Organismi | Rhizobium leguminosarum bv. viciae (strain 3841) |
Taxonomic identifieri | 216596 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Hyphomicrobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Nodulates the roots of pea plants as long as branched-chain amino acids Leu, Ile and Val (LIV) are added to the plant growth medium, but forms fewer nodules compared to wild-type. Nodules infected by the mutant are more spherical and contain more starch than those infected with wild-type, however the bacteroids appear visually normal.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_1000063813 | 1 – 202 | 3-isopropylmalate dehydratase small subunitAdd BLAST | 202 |
Interactioni
Subunit structurei
Heterodimer of LeuC and LeuD.
UniRule annotationProtein-protein interaction databases
STRINGi | 216596.RL4705 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0066, Bacteria |
HOGENOMi | CLU_081378_0_3_5 |
OMAi | AFTTHTG |
OrthoDBi | 1384217at2 |
Family and domain databases
CDDi | cd01577, IPMI_Swivel, 1 hit |
Gene3Di | 3.20.19.10, 1 hit |
HAMAPi | MF_01031, LeuD_type1, 1 hit |
InterProi | View protein in InterPro IPR004431, 3-IsopropMal_deHydase_ssu IPR015928, Aconitase/3IPM_dehydase_swvl IPR000573, AconitaseA/IPMdHydase_ssu_swvl IPR033940, IPMI_Swivel |
Pfami | View protein in Pfam PF00694, Aconitase_C, 1 hit |
TIGRFAMsi | TIGR00171, leuD, 1 hit |
i Sequence
Sequence statusi: Complete.
Q1MA52-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDKFVKLTGV AAPLPVVNVD TDMIIPKDYL KTIKRTGLGT GLFAEARYNE
60 70 80 90 100
DGSENPDFVL NKPAYRDAKI LVAGDNFGCG SSREHAPWAL LDFGIRCVIS
110 120 130 140 150
TSFADIFYNN CFKNGILPIK VSQEDLDKLM DDASRGSNAI LTVDLENLEI
160 170 180 190 200
TGPDGGLIKF DLDEFKRHCL LNGLDDIGLT LEKGKAIDSF EKKNAASHPW
AA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM236080 Genomic DNA Translation: CAK10188.1 |
RefSeqi | WP_003543984.1, NC_008380.1 |
Genome annotation databases
EnsemblBacteriai | CAK10188; CAK10188; RL4705 |
GeneIDi | 61426171 67485104 |
KEGGi | rle:RL4705 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM236080 Genomic DNA Translation: CAK10188.1 |
RefSeqi | WP_003543984.1, NC_008380.1 |
3D structure databases
SMRi | Q1MA52 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 216596.RL4705 |
Genome annotation databases
EnsemblBacteriai | CAK10188; CAK10188; RL4705 |
GeneIDi | 61426171 67485104 |
KEGGi | rle:RL4705 |
Phylogenomic databases
eggNOGi | COG0066, Bacteria |
HOGENOMi | CLU_081378_0_3_5 |
OMAi | AFTTHTG |
OrthoDBi | 1384217at2 |
Enzyme and pathway databases
UniPathwayi | UPA00048;UER00071 |
Family and domain databases
CDDi | cd01577, IPMI_Swivel, 1 hit |
Gene3Di | 3.20.19.10, 1 hit |
HAMAPi | MF_01031, LeuD_type1, 1 hit |
InterProi | View protein in InterPro IPR004431, 3-IsopropMal_deHydase_ssu IPR015928, Aconitase/3IPM_dehydase_swvl IPR000573, AconitaseA/IPMdHydase_ssu_swvl IPR033940, IPMI_Swivel |
Pfami | View protein in Pfam PF00694, Aconitase_C, 1 hit |
TIGRFAMsi | TIGR00171, leuD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LEUD_RHIL3 | |
Accessioni | Q1MA52Primary (citable) accession number: Q1MA52 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 5, 2008 |
Last sequence update: | May 30, 2006 | |
Last modified: | February 23, 2022 | |
This is version 89 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families