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O50078

- ACEA_HYPME

UniProt

O50078 - ACEA_HYPME

Protein

Isocitrate lyase

Gene

aceA

Organism
Hyphomicrobium methylovorum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Isocitrate = succinate + glyoxylate.1 Publication

    Cofactori

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

    Enzyme regulationi

    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.1 Publication

    Kineticsi

    1. KM=0.51 mM for D-isocitrate1 Publication

    pH dependencei

    Optimum pH is 7.5. The enzyme is stable when incubated for 15 min at 30 degrees Celsius at pH 7.5-9.1 Publication

    Temperature dependencei

    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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei225 – 2251By similarity

    GO - Molecular functioni

    1. isocitrate lyase activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. transition metal ion binding Source: UniProtKB

    GO - Biological processi

    1. glyoxylate cycle Source: UniProtKB
    2. tricarboxylic acid cycle Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-5154-MONOMER.
    UniPathwayiUPA00703; UER00719.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate lyaseImported (EC:4.1.3.1)
    Short name:
    ICLBy similarity
    Short name:
    IsocitraseBy similarity
    Short name:
    IsocitrataseBy similarity
    Gene namesi
    Name:aceABy similarity
    Synonyms:icl1 Publication
    OrganismiHyphomicrobium methylovorum
    Taxonomic identifieri84 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeHyphomicrobium

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 540539Isocitrate lyase1 PublicationPRO_0000389621Add
    BLAST

    Proteomic databases

    PRIDEiO50078.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO50078.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.60. 3 hits.
    InterProiIPR006254. Isocitrate_lyase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
    PfamiPF00463. ICL. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMiSSF51621. SSF51621. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O50078-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHKKTYSQL RSELLARYPV GLTKGGVSID DIVQLRLQSP YESHLDVARA    50
    MASVMRADMA AYDRDTGKFT QSLGCWSGFH AQQMIKAVKR LRGTTKGAYV 100
    YLSGWMVAGL RNRWGHLPDQ SMHEKTSVVD LIEEIYVSLR QADEVALNDL 150
    FNELKDARAK GATNKACEEI ISRIDGFESH VVPIIADIDA GFGNEHATYL 200
    LAKEMIKAGA CCLQIENQVS DAKQCGHQDG KVTVPREDFI EKLRACRLAF 250
    EELGVDDGVI VARTDSLGAS LTQKIPVSQQ AGDFASSYIK WLKTEPITDA 300
    NPLSEGELAI WQSGNFARPI RMPNGLFSFR EGTGRARVIE DCIASLKDGD 350
    ADLIWIETDT PNVDEIASMV AEIRKQVPDA KLVYNNSPSF NWTLNLRKQV 400
    RAQWISEGKI AEADYPDGTA LMSAQYDTSE LGREADDRLR QFQVDISARA 450
    GVFHNLITLP TFHLTAKSTD ELSHGYFGED RMLAYVATVQ REEIRRSISA 500
    VRHQHEVGSD LGDTFKEMVS GDRALKAGGA HNTMNQFAAE 540
    Length:540
    Mass (Da):59,898
    Last modified:June 1, 1998 - v1
    Checksum:iF289F07879534A7B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004651 Genomic DNA. Translation: BAA23678.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004651 Genomic DNA. Translation: BAA23678.1 .

    3D structure databases

    ProteinModelPortali O50078.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O50078.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00719 .
    BioCyci RETL1328306-WGS:GSTH-5154-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.60. 3 hits.
    InterProi IPR006254. Isocitrate_lyase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view ]
    PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
    Pfami PF00463. ICL. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
    SUPFAMi SSF51621. SSF51621. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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: GM2Imported.

    Entry informationi

    Entry nameiACEA_HYPME
    AccessioniPrimary (citable) accession number: O50078
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 60 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

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3