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A5GWH5 (LEUC_SYNR3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydratase large subunit
EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase
Gene names
Name:leuC
Ordered Locus Names:SynRCC307_2331
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01026

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01026

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01026

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4694693-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_1000063625

Sites

Metal binding3471Iron-sulfur (4Fe-4S) By similarity
Metal binding4071Iron-sulfur (4Fe-4S) By similarity
Metal binding4101Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GWH5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 7054F420917E80CE

FASTA46949,585
        10         20         30         40         50         60 
MSTATLYDKV WALHQVAELP SGSTQLFIGL HLIHEVTSPQ AFAALKDLGL SVRHPERTVA 

        70         80         90        100        110        120 
TVDHIVPTTS QARPFADGLA EEMLSTLERN CHENGIHLNG LGSGRQGIVH VMAPELGLTQ 

       130        140        150        160        170        180 
PGMTVACGDS HTSTHGAFGA IAFGIGTSQV RDVLASQSLT MNKLKVRRIW VDGALQPGVF 

       190        200        210        220        230        240 
AKDLVLHIIR TLGVKGGVGY AYEFAGPAIE ALSMEERMTL CNMAIEGGAR CGYVNPDQTT 

       250        260        270        280        290        300 
FDYLKGRPHA PSGDAWDHAV SWWKSLASGA DACFDDEVKF DAAVIAPTIT WGITPGQGIG 

       310        320        330        340        350        360 
VDEAVPTLEQ TPEEDRPLAQ EAYRYMDLQP GQAIAGLPVD VCFIGSCTNG RLSDLRAAAA 

       370        380        390        400        410        420 
VAAGRQVASG IKAFVVPGSE QVAAAAEAEG LDAVFRQAGF EWREPGCSMC LAMNPDRLEG 

       430        440        450        460 
RQISASSSNR NFKGRQGSAS GRTLLMSPAM VAAAAIAGRV TDVRSLPPA

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CT978603 Genomic DNA. Translation: CAK29234.1.
RefSeqYP_001228587.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GWH5.
ModBaseSearch...

Protein-protein interaction databases

STRING316278.SynRCC307_2331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK29234; CAK29234; SynRCC307_2331.
GeneID5156578.
KEGGsyr:SynRCC307_2331.
PATRIC23825617. VBISynSp108374_2343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMANWFRVPE.
ProtClustDBPRK05478.

Enzyme and pathway databases

UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01026. LeuC_type1.
InterProIPR004430. 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.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_SYNR3
AccessionPrimary (citable) accession number: A5GWH5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 12, 2007
Last modified: May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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