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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.UniRule annotation

Catalytic activityi

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation

Pathwayi: L-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  3. 3-isopropylmalate dehydrogenase (leuB)
  4. no protein annotated in this organism
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi347Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi407Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi410Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase large 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:leuCUniRule annotation
Ordered Locus Names:syc2197_d
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000768291 – 4683-isopropylmalate dehydratase large subunitAdd BLAST468

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

STRINGi269084.syc2197_d.

Structurei

3D structure databases

ProteinModelPortaliQ5MZY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CQI. Bacteria.
COG0065. LUCA.
HOGENOMiHOG000226972.
KOiK01703.
OMAiIDVCFIG.
OrthoDBiPOG091H02GD.

Family and domain databases

CDDicd01583. IPMI. 1 hit.
Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1. 1 hit.
InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR033941. IPMI_cat.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5MZY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGTLFDKV WDLHTVATLP SGQTQLFIGL HLIHEVTSPQ AFSMLRDRGL
60 70 80 90 100
TVKFPGRTVA TVDHIVPTEN QARPFADSLA EEMIVTLERN CRENGIRFYN
110 120 130 140 150
IGSGSQGIVH VIAPEQGLTQ PGMTIACGDS HTSTHGAFGA IAFGIGTSQV
160 170 180 190 200
RDVLASQTLA LSKLKVRKIE VNGELQPGVY AKDVILHIIR KLGVKGGVGY
210 220 230 240 250
AYEFAGSTFA AMSMEERMTV CNMAIEGGAR CGYVNPDQIT YDYLQGREFA
260 270 280 290 300
PQGEAWDRAI AWWESLRSEA DAEYDDVVVF DAAEIAPTVT WGITPGQGIG
310 320 330 340 350
ITETIPTPDS LLDEDRAVAA EAYSYMDLEP GAPLQGTKVD VCFIGSCTNG
360 370 380 390 400
RLSDLREAAK VAQGRKVAAG IKAFVVPGSE RVKQQAEAEG LDQIFTAAGF
410 420 430 440 450
EWRQAGCSMC LAMNPDKLEG RQISASSSNR NFKGRQGSAS GRTLLMSPAM
460
VAAAAIAGEV TDVRNWLN
Length:468
Mass (Da):50,343
Last modified:February 1, 2005 - v1
Checksum:i9D19B242070323BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD80387.1.
RefSeqiWP_011244507.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD80387; BAD80387; syc2197_d.
KEGGisyc:syc2197_d.
PATRICi32490540. VBISynElo117686_2500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD80387.1.
RefSeqiWP_011244507.1. NC_006576.1.

3D structure databases

ProteinModelPortaliQ5MZY3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269084.syc2197_d.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD80387; BAD80387; syc2197_d.
KEGGisyc:syc2197_d.
PATRICi32490540. VBISynElo117686_2500.

Phylogenomic databases

eggNOGiENOG4105CQI. Bacteria.
COG0065. LUCA.
HOGENOMiHOG000226972.
KOiK01703.
OMAiIDVCFIG.
OrthoDBiPOG091H02GD.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.

Family and domain databases

CDDicd01583. IPMI. 1 hit.
Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1. 1 hit.
InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR033941. IPMI_cat.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEUC_SYNP6
AccessioniPrimary (citable) accession number: Q5MZY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: November 30, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.