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O50078 (ACEA_HYPME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate lyase

Short name=ICL
Short name=Isocitrase
Short name=Isocitratase
EC=4.1.3.1
Gene names
Name:aceA
Synonyms:icl
OrganismHyphomicrobium methylovorum
Taxonomic identifier84 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeHyphomicrobium

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway. Ref.1

Catalytic activity

Isocitrate = succinate + glyoxylate. Ref.1

Cofactor

Divalent cations. Magnesium and, to a lesser extent, manganese. Ref.1

Enzyme regulation

In the presence of magnesium, inhibited by oxalate, potassium cyanide, manganese, silver, cadmium and to a lesser extent by succinate, glycolate, iodoacetamide, DL-penicillamine, aluminum, sodium, potassium, lithium and strontium. Ref.1

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. Ref.1

Subunit structure

Homotetramer. Ref.1

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.51 mM for D-isocitrate Ref.1

pH dependence:

Optimum pH is 7.5. The enzyme is stable when incubated for 15 min at 30 degrees Celsius at pH 7.5-9. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Loss of activity is 0%, 16%, 30%, 82% and 100% when incubated at 25, 30, 40, 50 and 60 degrees Celsius for 30 min, respectively. Ref.1

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from direct assay Ref.1. Source: UniProtKB

tricarboxylic acid cycle

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisocitrate lyase activity

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

transition metal ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 540539Isocitrate lyase Ref.1
PRO_0000389621

Sites

Active site2251 By similarity UniProtKB P0A9G6

Sequences

Sequence LengthMass (Da)Tools
O50078 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: F289F07879534A7B

FASTA54059,898
        10         20         30         40         50         60 
MAHKKTYSQL RSELLARYPV GLTKGGVSID DIVQLRLQSP YESHLDVARA MASVMRADMA 

        70         80         90        100        110        120 
AYDRDTGKFT QSLGCWSGFH AQQMIKAVKR LRGTTKGAYV YLSGWMVAGL RNRWGHLPDQ 

       130        140        150        160        170        180 
SMHEKTSVVD LIEEIYVSLR QADEVALNDL FNELKDARAK GATNKACEEI ISRIDGFESH 

       190        200        210        220        230        240 
VVPIIADIDA GFGNEHATYL LAKEMIKAGA CCLQIENQVS DAKQCGHQDG KVTVPREDFI 

       250        260        270        280        290        300 
EKLRACRLAF EELGVDDGVI VARTDSLGAS LTQKIPVSQQ AGDFASSYIK WLKTEPITDA 

       310        320        330        340        350        360 
NPLSEGELAI WQSGNFARPI RMPNGLFSFR EGTGRARVIE DCIASLKDGD ADLIWIETDT 

       370        380        390        400        410        420 
PNVDEIASMV AEIRKQVPDA KLVYNNSPSF NWTLNLRKQV RAQWISEGKI AEADYPDGTA 

       430        440        450        460        470        480 
LMSAQYDTSE LGREADDRLR QFQVDISARA GVFHNLITLP TFHLTAKSTD ELSHGYFGED 

       490        500        510        520        530        540 
RMLAYVATVQ REEIRRSISA VRHQHEVGSD LGDTFKEMVS GDRALKAGGA HNTMNQFAAE 

« Hide

References

[1]"Characterization, gene cloning and expression of isocitrate lyase involved in the assimilation of one-carbon compounds in Hyphomicrobium methylovorum GM2."
Tanaka Y., Yoshida T., Watanabe K., Izumi Y., Mitsunaga T.
Eur. J. Biochem. 249:820-825(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT.
Strain: GM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004651 Genomic DNA. Translation: BAA23678.1.

3D structure databases

ProteinModelPortalO50078.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO50078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-5154-MONOMER.
UniPathwayUPA00703; UER00719.

Family and domain databases

Gene3D3.20.20.60. 3 hits.
InterProIPR006254. Isocitrate_lyase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 3 hits.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 2 hits.
ProtoNetSearch...

Entry information

Entry nameACEA_HYPME
AccessionPrimary (citable) accession number: O50078
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways