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O50078

- ACEA_HYPME

UniProt

O50078 - ACEA_HYPME

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Protein

Isocitrate lyase

Gene

aceA

Organism
Hyphomicrobium methylovorum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations. Mg(2+) or, to a lesser extent, Mn(2+).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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MAHKKTYSQL RSELLARYPV GLTKGGVSID DIVQLRLQSP YESHLDVARA
60 70 80 90 100
MASVMRADMA AYDRDTGKFT QSLGCWSGFH AQQMIKAVKR LRGTTKGAYV
110 120 130 140 150
YLSGWMVAGL RNRWGHLPDQ SMHEKTSVVD LIEEIYVSLR QADEVALNDL
160 170 180 190 200
FNELKDARAK GATNKACEEI ISRIDGFESH VVPIIADIDA GFGNEHATYL
210 220 230 240 250
LAKEMIKAGA CCLQIENQVS DAKQCGHQDG KVTVPREDFI EKLRACRLAF
260 270 280 290 300
EELGVDDGVI VARTDSLGAS LTQKIPVSQQ AGDFASSYIK WLKTEPITDA
310 320 330 340 350
NPLSEGELAI WQSGNFARPI RMPNGLFSFR EGTGRARVIE DCIASLKDGD
360 370 380 390 400
ADLIWIETDT PNVDEIASMV AEIRKQVPDA KLVYNNSPSF NWTLNLRKQV
410 420 430 440 450
RAQWISEGKI AEADYPDGTA LMSAQYDTSE LGREADDRLR QFQVDISARA
460 470 480 490 500
GVFHNLITLP TFHLTAKSTD ELSHGYFGED RMLAYVATVQ REEIRRSISA
510 520 530 540
VRHQHEVGSD LGDTFKEMVS GDRALKAGGA HNTMNQFAAE
Length:540
Mass (Da):59,898
Last modified:June 1, 1998 - v1
Checksum:iF289F07879534A7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004651 Genomic DNA. Translation: BAA23678.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 62 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