P0A9G6 (ACEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity.
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; (S)-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.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glyoxylate cycle Inferred by curator PubMed 366070. Source: EcoliWiki tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cation binding Inferred from direct assay Ref.10. Source: EcoliWiki isocitrate lyase activity Inferred from direct assay Ref.10. Source: EcoliWiki
Complete GO annotation...

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

1

Probable

Experimental info

Mutagenesis

195

1

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

Mutagenesis

195

1

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

Sequence conflict

101 – 117

17

LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416. Ref.3

Sequence conflict

215

1

A → P in CAA30416. Ref.3

Sequence conflict

293

1

P → R in AAA24009. Ref.8

Sequence conflict

338

1

Q → E in CAA30416. Ref.3

Sequence conflict

419 – 434

16

TSSVT…EESQF → DVFSHRADRLH Ref.4

Secondary structure

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434

Helix Strand Turn

Details...

Helix

4 – 14

11

Helix

18 – 20

3

Helix

29 – 34

6

Helix

44 – 57

14

Turn

58 – 60

3

Beta strand

61 – 70

10

Helix

74 – 83

10

Beta strand

88 – 90

3

Helix

92 – 98

7

Beta strand

108 – 110

3

Helix

116 – 137

22

Beta strand

154 – 157

4

Beta strand

162 – 164

3

Helix

165 – 177

13

Beta strand

181 – 188

8

Helix

190 – 192

3

Helix

206 – 223

18

Beta strand

228 – 233

6

Turn

235 – 237

3

Beta strand

240 – 242

3

Helix

247 – 252

6

Beta strand

253 – 257

5

Beta strand

263 – 265

3

Helix

269 – 279

11

Helix

280 – 282

3

Beta strand

284 – 288

5

Helix

295 – 308

14

Beta strand

313 – 317

5

Helix

336 – 343

8

Beta strand

345 – 350

6

Helix

353 – 371

19

Helix

374 – 381

8

Helix

383 – 390

8

Turn

391 – 393

3

Helix

399 – 402

4

Helix

405 – 415

11

Sequences

	Sequence		Length	Mass (Da)
	P0A9G6 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: F66449CCD1E168E9	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

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] [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]	"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] [Europe PMC] [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] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_418439.1. NC_000913.2.
YP_492158.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P0A9G6.

SMR

P0A9G6. Positions 2-417.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35893N.

IntAct

P0A9G6. 3 interactions.

STRING

511145.b4015.

2D gel databases

SWISS-2DPAGE

P0A9G6.

Proteomic databases

PaxDb

P0A9G6.

PRIDE

P0A9G6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76985; AAC76985; b4015.
BAE78017; BAE78017; BAE78017.

GeneID

12934475.
948517.

KEGG

ecj:Y75_p3902.
eco:b4015.

PATRIC

32123557. VBIEscCol129921_4127.

Organism-specific databases

EchoBASE

EB0021.

EcoGene

EG10022. aceA.

Phylogenomic databases

eggNOG

COG2224.

HOGENOM

HOG000238475.

KO

K01637.

OMA

QAVQQVK.

ProtClustDB

PRK15063.

Enzyme and pathway databases

BioCyc

EcoCyc:ISOCIT-LYASE-MONOMER.
ECOL316407:JW3975-MONOMER.
MetaCyc:ISOCIT-LYASE-MONOMER.

UniPathway

UPA00703; UER00719.

Gene expression databases

Genevestigator

P0A9G6.

Family and domain databases

Gene3D

3.20.20.60. 1 hit.

InterPro

IPR006254. Isocitrate_lyase.
IPR000918. Isocitrate_lyase/Pmutase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]

PANTHER

PTHR21631:SF3. PTHR21631:SF3. 1 hit.

Pfam

PF00463. ICL. 2 hits.
[Graphical view]

PIRSF

PIRSF001362. Isocit_lyase. 1 hit.

SUPFAM

SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

TIGRFAMs

TIGR01346. isocit_lyase. 2 hits.

PROSITE

PS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9G6.

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:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program