Q4HYR2 (ACEA_GIBZE) 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:	ICL1
ORF Names:	FGSG_09896

Organism

Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum) [Reference proteome]

Taxonomic identifier

229533 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Gibberella › Gibberella zeae

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Isocitrate = succinate + glyoxylate.
Pathway	Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.
Subunit structure	Homotetramer By similarity.
Subcellular location	Peroxisome By similarity.
Sequence similarities	Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Peroxisome
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	isocitrate lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 546	546	Isocitrate lyase		PRO_0000286157
Sites
	Active site	215	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4HYR2 [UniParc]. Last modified August 16, 2005. Version 1. Checksum: C90BD9BFBAB4BE9D	FASTA	546	60,826
	10 20 30 40 50 60 MASQNMTNPS INPDIEDELF QKEVEAVKTW WSDSRWRQTK RPFTAEQIVS KRGYLPIDYA 70 80 90 100 110 120 SNTQAKKLWK ILEHRFENRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASASDEP 130 140 150 160 170 180 GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ RQERLSVPKE QRANLLNIDY LRPIVADADT 190 200 210 220 230 240 GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA 250 260 270 280 290 300 DIMGSDLLAI ARTDAEAATL LSTNIDPRDH AFILGSTNST LKPLNDLMIA AEATGKSGAE 310 320 330 340 350 360 LQRIEDEWLA KANLSSFDDA VAAAIDAGSF SDKAGIKQEY TSRAKGKSNF EARAVARQLL 370 380 390 400 410 420 GRDIFFDWDA PRTREGYFRL KGGCDCAVNR AIAYAPYCDA IWMESKLPDF AQAEQFAQGV 430 440 450 460 470 480 HAVWPEKKLA YNLSPSFNWK TAMPRDEQET YIRRLAKLGY CWQFITLAGL HTTALISDQF 490 500 510 520 530 540 AKAYSTVGMR AYGELVQEPE MDQKVDVVKH QKWSGATYVD ELQKMVTGGI SSTAAMGAGV TEDQFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization." Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S. , Goswami R.S., Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C. Science 317:1400-1402(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.
[2]	"Comparative genomics reveals mobile pathogenicity chromosomes in Fusarium." Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., Antoniw J., Baker S.E. , Bluhm B.H., Breakspear A., Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., Rep M. Nature 464:367-373(2010) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084.

Cross-references

Sequence databases
RefSeq	XP_390072.1. XM_390072.1.
3D structure databases
HSSP	HSSP built from PDB template 1F8M based on UniProtKB P0A5H3.
ProteinModelPortal	Q4HYR2.
SMR	Q4HYR2. Positions 16-529.
ModBase	Search...
Protein-protein interaction databases
STRING	5518.FG09896.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	FGSG_09896T0; FGSG_09896P0; FGSG_09896.
GeneID	2791934.
KEGG	fgr:FG09896.1.
Phylogenomic databases
eggNOG	COG2224.
KO	K01637.
Enzyme and pathway databases
UniPathway	UPA00703; UER00719.
Family and domain databases
Gene3D	3.20.20.60. 2 hits.
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. 1 hit. [Graphical view]
PIRSF	PIRSF001362. Isocit_lyase. 1 hit.
SUPFAM	SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01346. isocit_lyase. 1 hit.
PROSITE	PS00161. ISOCITRATE_LYASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACEA_GIBZE

Accession

Primary (citable) accession number: Q4HYR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	August 16, 2005
Last modified:	April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program