Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A9G6

- ACEA_ECOLI

UniProt

P0A9G6 - ACEA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Isocitrate lyase

Gene

aceA

Organism
Escherichia coli (strain K12)
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 (By similarity).By similarity

Catalytic activityi

Isocitrate = succinate + glyoxylate.PROSITE-ProRule annotation

Cofactori

Divalent cations.

Enzyme regulationi

Is activated by phosphorylation (on histidine) and is inhibited by PEP, 3-phosphoglycerate and succinate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei195 – 1951Curated

GO - Molecular functioni

  1. cation binding Source: EcoliWiki
  2. isocitrate lyase activity Source: EcoliWiki

GO - Biological processi

  1. glyoxylate cycle Source: EcoliWiki
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciEcoCyc:ISOCIT-LYASE-MONOMER.
ECOL316407:JW3975-MONOMER.
MetaCyc:ISOCIT-LYASE-MONOMER.
UniPathwayiUPA00703; UER00719.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate lyase (EC:4.1.3.1)
Short name:
ICL
Short name:
Isocitrase
Short name:
Isocitratase
Gene namesi
Name:aceA
Synonyms:icl
Ordered Locus Names:b4015, JW3975
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10022. aceA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951C → A: Large decrease in activity. 1 Publication
Mutagenesisi195 – 1951C → S: Large decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Isocitrate lyasePRO_0000068774Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0A9G6.
PRIDEiP0A9G6.

2D gel databases

SWISS-2DPAGEP0A9G6.

Expressioni

Gene expression databases

GenevestigatoriP0A9G6.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-35893N.
IntActiP0A9G6. 3 interactions.
STRINGi511145.b4015.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411
Helixi18 – 203
Helixi29 – 346
Helixi44 – 5714
Turni58 – 603
Beta strandi61 – 7010
Helixi74 – 8310
Beta strandi88 – 903
Helixi92 – 987
Beta strandi108 – 1103
Helixi116 – 13722
Beta strandi154 – 1574
Beta strandi162 – 1643
Helixi165 – 17713
Beta strandi181 – 1888
Helixi190 – 1923
Helixi206 – 22318
Beta strandi228 – 2336
Turni235 – 2373
Beta strandi240 – 2423
Helixi247 – 2526
Beta strandi253 – 2575
Beta strandi263 – 2653
Helixi269 – 27911
Helixi280 – 2823
Beta strandi284 – 2885
Helixi295 – 30814
Beta strandi313 – 3175
Helixi336 – 3438
Beta strandi345 – 3506
Helixi353 – 37119
Helixi374 – 3818
Helixi383 – 3908
Turni391 – 3933
Helixi399 – 4024
Helixi405 – 41511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGWX-ray2.10A/B/C/D1-434[»]
ProteinModelPortaliP0A9G6.
SMRiP0A9G6. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9G6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2224.
HOGENOMiHOG000238475.
InParanoidiP0A9G6.
KOiK01637.
OMAiDQIQWAN.
OrthoDBiEOG689HMX.
PhylomeDBiP0A9G6.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
InterProiIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamiPF00463. ICL. 2 hits.
[Graphical view]
PIRSFiPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR01346. isocit_lyase. 2 hits.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9G6 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA
60 70 80 90 100
AKMWRLLHGE SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN
110 120 130 140 150
LAASMYPDQS LYPANSVPAV VERINNTFRR ADQIQWSAGI EPGDPRYVDY
160 170 180 190 200
FLPIVADAEA GFGGVLNAFE LMKAMIEAGA AAVHFEDQLA SVKKCGHMGG
210 220 230 240 250
KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL ITSDCDPYDS
260 270 280 290 300
EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
310 320 330 340 350
FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI
360 370 380 390 400
TLAGIHSMWF NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ
410 420 430
QEVGTGYFDK VTTIIQGGTS SVTALTGSTE ESQF
Length:434
Mass (Da):47,522
Last modified:July 19, 2005 - v1
Checksum:iF66449CCD1E168E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 11717LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416. (PubMed:3290857)CuratedAdd
BLAST
Sequence conflicti215 – 2151A → P in CAA30416. (PubMed:3290857)Curated
Sequence conflicti293 – 2931P → R in AAA24009. (PubMed:2836370)Curated
Sequence conflicti338 – 3381Q → E in CAA30416. (PubMed:3290857)Curated
Sequence conflicti419 – 43416TSSVT…EESQF → DVFSHRADRLH(PubMed:3049537)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12431 Genomic DNA. Translation: CAA30974.1.
X07543 Genomic DNA. Translation: CAA30416.1.
M22621 Genomic DNA. Translation: AAC13650.1.
U00006 Genomic DNA. Translation: AAC43109.1.
U00096 Genomic DNA. Translation: AAC76985.1.
AP009048 Genomic DNA. Translation: BAE78017.1.
M20714 Genomic DNA. Translation: AAA24009.1.
PIRiS05692. WZECIC.
RefSeqiNP_418439.1. NC_000913.3.
YP_492158.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76985; AAC76985; b4015.
BAE78017; BAE78017; BAE78017.
GeneIDi12934475.
948517.
KEGGiecj:Y75_p3902.
eco:b4015.
PATRICi32123557. VBIEscCol129921_4127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12431 Genomic DNA. Translation: CAA30974.1 .
X07543 Genomic DNA. Translation: CAA30416.1 .
M22621 Genomic DNA. Translation: AAC13650.1 .
U00006 Genomic DNA. Translation: AAC43109.1 .
U00096 Genomic DNA. Translation: AAC76985.1 .
AP009048 Genomic DNA. Translation: BAE78017.1 .
M20714 Genomic DNA. Translation: AAA24009.1 .
PIRi S05692. WZECIC.
RefSeqi NP_418439.1. NC_000913.3.
YP_492158.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IGW X-ray 2.10 A/B/C/D 1-434 [» ]
ProteinModelPortali P0A9G6.
SMRi P0A9G6. Positions 2-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35893N.
IntActi P0A9G6. 3 interactions.
STRINGi 511145.b4015.

2D gel databases

SWISS-2DPAGE P0A9G6.

Proteomic databases

PaxDbi P0A9G6.
PRIDEi P0A9G6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76985 ; AAC76985 ; b4015 .
BAE78017 ; BAE78017 ; BAE78017 .
GeneIDi 12934475.
948517.
KEGGi ecj:Y75_p3902.
eco:b4015.
PATRICi 32123557. VBIEscCol129921_4127.

Organism-specific databases

EchoBASEi EB0021.
EcoGenei EG10022. aceA.

Phylogenomic databases

eggNOGi COG2224.
HOGENOMi HOG000238475.
InParanoidi P0A9G6.
KOi K01637.
OMAi DQIQWAN.
OrthoDBi EOG689HMX.
PhylomeDBi P0A9G6.

Enzyme and pathway databases

UniPathwayi UPA00703 ; UER00719 .
BioCyci EcoCyc:ISOCIT-LYASE-MONOMER.
ECOL316407:JW3975-MONOMER.
MetaCyc:ISOCIT-LYASE-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A9G6.
PROi P0A9G6.

Gene expression databases

Genevestigatori P0A9G6.

Family and domain databases

Gene3Di 3.20.20.60. 1 hit.
InterProi IPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
PANTHERi PTHR21631:SF3. PTHR21631:SF3. 1 hit.
Pfami PF00463. ICL. 2 hits.
[Graphical view ]
PIRSFi PIRSF001362. Isocit_lyase. 1 hit.
SUPFAMi SSF51621. SSF51621. 1 hit.
TIGRFAMsi TIGR01346. isocit_lyase. 2 hits.
PROSITEi PS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
    Byrne C.R., Stokes H.W., Ward K.A.
    Nucleic Acids Res. 16:9342-9342(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli."
    Byrne C.R., Stokes H.W., Ward K.A.
    Nucleic Acids Res. 16:10924-10924(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Nucleotide sequence of the aceA gene coding for isocitrate lyase in Escherichia coli."
    Rieul C., Bleicher F., Duclos B., Cortay J.-C., Cozzone A.J.
    Nucleic Acids Res. 16:5689-5689(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli."
    Matsuoka M., McFadden B.A.
    J. Bacteriol. 170:4528-4536(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase."
    Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., Laporte D.C.
    J. Bacteriol. 170:2763-2769(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 293-434.
  9. "Evidence of histidine phosphorylation in isocitrate lyase from Escherichia coli."
    Robertson E.F., Hoyt J.C., Reeves H.C.
    J. Biol. Chem. 263:2477-2482(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  10. "Escherichia coli isocitrate lyase: properties and comparisons."
    Hoyt J.C., Robertson E.F., Berlyn K.A., Reeves H.C.
    Biochim. Biophys. Acta 966:30-35(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308."
    Robertson A.G., Nimmo H.G.
    Biochem. J. 305:239-244(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-195.
    Strain: ML308.

Entry informationi

Entry nameiACEA_ECOLI
AccessioniPrimary (citable) accession number: P0A9G6
Secondary accession number(s): P05313, Q2M6T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 83 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3