Isocitrate lyase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A9G6 (ACEA_ECOLI)

Last modified June 16, 2009. Version 39. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Isocitrate lyase
      Short name=ICL
      Short name=Isocitratase
      Short name=Isocitrase
    EC=4.1.3.1

Gene names

Name:	aceA
Synonyms:	icl
Ordered Locus Names:	b4015, JW3975

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Isocitrate = succinate + glyoxylate.
Cofactor	Divalent cations.
Enzyme regulation	Is activated by phosphorylation (on histidine) and is inhibited by PEP, 3-phosphoglycerate and succinate.
Pathway	Carbohydrate metabolism; glyoxylate cycle; L-malate from isocitrate: step 1/2.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

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Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	isocitrate lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Isocitrate lyase

PRO_0000068774

Sites

Active site

195

Probable

Experimental info

Mutagenesis

195

C → A: Large decrease in activity. Ref.11

Mutagenesis

195

C → S: Large decrease in activity. Ref.11

Sequence conflict

101 – 117

LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416. Ref.3

Sequence conflict

215

A → P in CAA30416. Ref.3

Sequence conflict

293

P → R in AAA24009. Ref.8

Sequence conflict

338

Q → E in CAA30416. Ref.3

Sequence conflict

419 – 434

TSSVT…EESQF → DVFSHRADRLH Ref.4

Secondary structure

434

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A9G6-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: F66449CCD1E168E9
Show »

FASTA

434

47,522

        10         20         30         40         50         60 
MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA AKMWRLLHGE 

        70         80         90        100        110        120 
SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN LAASMYPDQS LYPANSVPAV 

       130        140        150        160        170        180 
VERINNTFRR ADQIQWSAGI EPGDPRYVDY FLPIVADAEA GFGGVLNAFE LMKAMIEAGA 

       190        200        210        220        230        240 
AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL 

       250        260        270        280        290        300 
ITSDCDPYDS EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR 

       310        320        330        340        350        360 
FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI TLAGIHSMWF 

       370        380        390        400        410        420 
NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGTS 

       430 
SVTALTGSTE ESQF

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3050899] [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: 3060852] [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: 3290857] [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: 3049537] [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: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 2836370] [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: 3276689] [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: 3291954] [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: 7826335] [Abstract] Cited for: MUTAGENESIS OF CYS-195. Strain: ML308.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

PIR

WZECIC. S05692.

RefSeq

AP_004516.1.
NP_418439.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IGW	X-ray	2.10	A/B/C/D	1-434	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P0A9G6.

2DBase-Ecoli

P0A9G6.

Genome annotation databases

GeneID

948517.

GenomeReviews

Gene locus JW3975 in contig AP009048_GR.
Gene locus b4015 in contig U00096_GR.

KEGG

ecj:JW3975.
eco:b4015.

Organism-specific databases

EchoBASE

EB0021.

EcoGene

EG10022. aceA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9G6.

OMA

P0A9G6. LVWCETG.

Enzyme and pathway databases

BioCyc

EcoCyc:ISOCIT-LYASE-MON.
MetaCyc:ISOCIT-LYASE-MON.

Family and domain databases

InterPro

IPR006254. Isocitrate_lyase.
IPR000918. Isocitrate_lyase_ph.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]

Gene3D

G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

PANTHER

PTHR21631:SF3. Isocit_lyase. 1 hit.

Pfam

PF00463. ICL. 1 hit.
[Graphical view]

PIRSF

PIRSF001362. Isocit_lyase. 1 hit.

ProDom

PD001857. Isocit_lyase_ph. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01346. isocit_lyase. 1 hit.

PROSITE

PS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

ACEA_ECOLI

Accession

Primary (citable) accession number: P0A9G6
Secondary accession number(s): P05313, Q2M6T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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