UniProtKB - P0CT06 (ACEA_MAGO7)

BLAST

>sp|P0CT06|ACEA_MAGO7 Isocitrate lyase OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=ICL1 PE=1 SV=1
MASKNMVNPAVEPSMEDDLFAREVAEVKQWWSDPRWRYTKRPFTAEQIVSKRGNLKIEYP
SNAQSKKLWKILEGRFQKRDASYTYGCLEPTMVTQMAKYLDTVYVSGWQSSSTASSSDEP
GPDLADYPYTTVPNKVSHLFMAQLFHDRKQRHERLSAPKSERSKLQNIDYLRPIIADADT
GHGGLTAVMKLTKLFIEKGAAGIHIEDQAPGTKKCGHMAGKVLVPISEHINRLVAIRAQA
DIMGVDLLAIARTDAEAATLITTSIDPRDHAFILGCTNPSLQPLADLMNTAEQSGKTGDQ
LQAIEDEWMAKANLKRFDDAVVDVINSSSSIRNPKDVAAKYLQAAKGKSNREARAIASSL
GVPEIFFDWDSPRTREGYFRIKGGCDCAINRAIAYAPYADAIWMESKLPDYEQAKEFAEG
VHAVYPEQKLAYNLSPSFNWKTAMPRDEQETYIRRLAGLGYCWQFITLAGLHTTALISDR
FARAYSEVGMRAYGELVQEPEMELGVDVVKHQKWSGATYVDELQKMVTGGVSSTAAMGKG
VTEDQFH

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History
Entry version 32 (07 Nov 2018)
Sequence version 1 (18 Sep 2013)
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Protein

Isocitrate lyase

Gene

ICL1

Organism

Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate (By similarity). plays an important role in plant pathogenicity.By similarity1 Publication

Catalytic activityⁱ

Isocitrate = succinate + glyoxylate.By similarity

(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.By similarity

Cofactorⁱ

Mg²⁺By similarity

Pathwayⁱ: glyoxylate cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from isocitrate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Isocitrate lyase (ICL1)
Malate synthase (MGG_02813)

This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	177	MagnesiumBy similarity	1
Active siteⁱ	215	Proton acceptorBy similarity	1
Binding siteⁱ	252	SubstrateBy similarity	1
Binding siteⁱ	467	SubstrateBy similarity	1

GO - Molecular functionⁱ

isocitrate lyase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW
methylisocitrate lyase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glyoxylate cycle Source: UniProtKB-UniPathway
tricarboxylic acid cycle Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Glyoxylate bypass, Tricarboxylic acid cycle
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayⁱ	UPA00703;UER00719

UniPathwayⁱ

UPA00703;UER00719

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Isocitrate lyase1 Publication (EC:4.1.3.1By similarity) Short name: ICLCurated Short name: IsocitraseCurated Short name: IsocitrataseCurated Alternative name(s): Methylisocitrate lyaseBy similarity (EC:4.1.3.30By similarity) Short name: MICACurated Threo-D(S)-isocitrate glyoxylate-lyaseCurated
Gene namesⁱ	Name:ICL11 Publication ORF Names:MGG_04895
Organismⁱ	Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic identifierⁱ	242507 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe › Magnaporthe oryzae
Proteomesⁱ	UP000009058 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	FungiDB:MGG_04895

EuPathDBⁱ

FungiDB:MGG_04895

Keywords - Cellular componentⁱ

Glyoxysome, Peroxisome

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Leads to reduced virulence and a delay in the expression of rice blast symptoms.1 Publication

Chemistry databases

ChEMBLⁱ	CHEMBL1075264

ChEMBLⁱ

CHEMBL1075264

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000068793	1 – 547	Isocitrate lyaseAdd BLAST		547

Proteomic databases

PRIDEⁱ	P0CT06

PRIDEⁱ

P0CT06

Interactionⁱ

Subunit structureⁱ

Homotetramer.By similarity

Protein-protein interaction databases

STRINGⁱ	318829.MGG_04895T0

STRINGⁱ

318829.MGG_04895T0

Chemistry databases

BindingDBⁱ

P0CT06

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	13 – 15	Combined sources	3
Helixⁱ	16 – 31	Combined sources	16
Helixⁱ	34 – 36	Combined sources	3
Helixⁱ	45 – 49	Combined sources	5
Helixⁱ	60 – 78	Combined sources	19
Beta strandⁱ	82 – 86	Combined sources	5
Helixⁱ	90 – 96	Combined sources	7
Turnⁱ	97 – 99	Combined sources	3
Beta strandⁱ	103 – 105	Combined sources	3
Helixⁱ	107 – 113	Combined sources	7
Beta strandⁱ	122 – 125	Combined sources	4
Helixⁱ	131 – 156	Combined sources	26
Helixⁱ	159 – 164	Combined sources	6
Beta strandⁱ	174 – 177	Combined sources	4
Beta strandⁱ	182 – 184	Combined sources	3
Helixⁱ	185 – 198	Combined sources	14
Beta strandⁱ	201 – 208	Combined sources	8
Turnⁱ	210 – 212	Combined sources	3
Beta strandⁱ	218 – 220	Combined sources	3
Helixⁱ	226 – 243	Combined sources	18
Beta strandⁱ	248 – 253	Combined sources	6
Turnⁱ	255 – 257	Combined sources	3
Beta strandⁱ	260 – 262	Combined sources	3
Helixⁱ	267 – 269	Combined sources	3
Turnⁱ	270 – 272	Combined sources	3
Helixⁱ	284 – 292	Combined sources	9
Helixⁱ	299 – 312	Combined sources	14
Helixⁱ	317 – 325	Combined sources	9
Helixⁱ	334 – 345	Combined sources	12
Helixⁱ	350 – 359	Combined sources	10
Beta strandⁱ	368 – 370	Combined sources	3
Beta strandⁱ	379 – 381	Combined sources	3
Helixⁱ	385 – 395	Combined sources	11
Helixⁱ	396 – 398	Combined sources	3
Beta strandⁱ	400 – 404	Combined sources	5
Helixⁱ	411 – 422	Combined sources	12
Beta strandⁱ	430 – 433	Combined sources	4
Helixⁱ	440 – 443	Combined sources	4
Helixⁱ	446 – 458	Combined sources	13
Beta strandⁱ	461 – 466	Combined sources	6
Helixⁱ	469 – 488	Combined sources	20
Helixⁱ	490 – 496	Combined sources	7
Helixⁱ	498 – 504	Combined sources	7
Helixⁱ	507 – 509	Combined sources	3
Helixⁱ	511 – 514	Combined sources	4
Helixⁱ	517 – 526	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P0CT06
SMRⁱ	P0CT06
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	106 – 108	Substrate bindingBy similarity	3
Regionⁱ	216 – 217	Substrate bindingBy similarity	2
Regionⁱ	433 – 437	Substrate bindingBy similarity	5

Sequence similaritiesⁱ

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.Curated

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K01637
OMAⁱ	LEKDWAE
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C19UX

Family and domain databases

InterProⁱ	View protein in InterPro IPR006254 Isocitrate_lyase IPR018523 Isocitrate_lyase_ph_CS IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
PANTHERⁱ	PTHR21631 PTHR21631, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00463 ICL, 1 hit
PIRSFⁱ	PIRSF001362 Isocit_lyase, 1 hit
SUPFAMⁱ	SSF51621 SSF51621, 1 hit
TIGRFAMsⁱ	TIGR01346 isocit_lyase, 1 hit
PROSITEⁱ	View protein in PROSITE PS00161 ISOCITRATE_LYASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0CT06-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MASKNMVNPA VEPSMEDDLF AREVAEVKQW WSDPRWRYTK RPFTAEQIVS 
        60         70         80         90        100
KRGNLKIEYP SNAQSKKLWK ILEGRFQKRD ASYTYGCLEP TMVTQMAKYL 
       110        120        130        140        150
DTVYVSGWQS SSTASSSDEP GPDLADYPYT TVPNKVSHLF MAQLFHDRKQ 
       160        170        180        190        200
RHERLSAPKS ERSKLQNIDY LRPIIADADT GHGGLTAVMK LTKLFIEKGA 
       210        220        230        240        250
AGIHIEDQAP GTKKCGHMAG KVLVPISEHI NRLVAIRAQA DIMGVDLLAI 
       260        270        280        290        300
ARTDAEAATL ITTSIDPRDH AFILGCTNPS LQPLADLMNT AEQSGKTGDQ 
       310        320        330        340        350
LQAIEDEWMA KANLKRFDDA VVDVINSSSS IRNPKDVAAK YLQAAKGKSN 
       360        370        380        390        400
REARAIASSL GVPEIFFDWD SPRTREGYFR IKGGCDCAIN RAIAYAPYAD 
       410        420        430        440        450
AIWMESKLPD YEQAKEFAEG VHAVYPEQKL AYNLSPSFNW KTAMPRDEQE 
       460        470        480        490        500
TYIRRLAGLG YCWQFITLAG LHTTALISDR FARAYSEVGM RAYGELVQEP 
       510        520        530        540 
EMELGVDVVK HQKWSGATYV DELQKMVTGG VSSTAAMGKG VTEDQFH

Length:547

Mass (Da):61,001

Last modified:September 18, 2013 - v1

Checksum:ⁱ0BF3F9921E04D1D0

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF540383 Genomic DNA Translation: AAN28719.1 CM001233 Genomic DNA Translation: EHA52574.1
NCBI Reference Sequences More...RefSeqⁱ	XP_003712381.1, XM_003712333.1

Genome annotation databases

EnsemblFungiⁱ	MGG_04895T0; MGG_04895T0; MGG_04895
GeneIDⁱ	2675603
KEGGⁱ	mgr:MGG_04895

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0CT06	Isocitrate lyase		MAGOY		547	UniRef90_P0CT06
UPI0007B176A2		MAGO7		560
UPI0007B17697		MAGO7		560

Protein	Similar proteins		Species	Score	Length	Source
P0CT06	Isocitrate lyase		YEAST		557	UniRef50_P28240
Isocitrate lyase		GOSHI		576
Isocitrate lyase		RICCO		576
Isocitrate lyase		BRANA		576
Isocitrate lyase		ARATH		576
+421

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF540383 Genomic DNA Translation: AAN28719.1 CM001233 Genomic DNA Translation: EHA52574.1
RefSeqⁱ	XP_003712381.1, XM_003712333.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5E9F	X-ray	2.80	A/B/C/D	1-547	[»]
	5E9G	X-ray	2.10	A/B/C/D	1-547	[»]
ProteinModelPortalⁱ	P0CT06
SMRⁱ	P0CT06
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	318829.MGG_04895T0

STRINGⁱ

318829.MGG_04895T0

Chemistry databases

BindingDBⁱ	P0CT06
ChEMBLⁱ	CHEMBL1075264

Proteomic databases

PRIDEⁱ	P0CT06

PRIDEⁱ

P0CT06

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	MGG_04895T0; MGG_04895T0; MGG_04895
GeneIDⁱ	2675603
KEGGⁱ	mgr:MGG_04895

Organism-specific databases

EuPathDBⁱ	FungiDB:MGG_04895

EuPathDBⁱ

FungiDB:MGG_04895

Phylogenomic databases

KOⁱ	K01637
OMAⁱ	LEKDWAE
OrthoDBⁱ	EOG092C19UX

Enzyme and pathway databases

UniPathwayⁱ	UPA00703;UER00719

UniPathwayⁱ

UPA00703;UER00719

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0CT06

PROⁱ

PR:P0CT06

Family and domain databases

InterProⁱ	View protein in InterPro IPR006254 Isocitrate_lyase IPR018523 Isocitrate_lyase_ph_CS IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
PANTHERⁱ	PTHR21631 PTHR21631, 1 hit
Pfamⁱ	View protein in Pfam PF00463 ICL, 1 hit
PIRSFⁱ	PIRSF001362 Isocit_lyase, 1 hit
SUPFAMⁱ	SSF51621 SSF51621, 1 hit
TIGRFAMsⁱ	TIGR01346 isocit_lyase, 1 hit
PROSITEⁱ	View protein in PROSITE PS00161 ISOCITRATE_LYASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACEA_MAGO7
Accessionⁱ	P0CT06Primary (citable) accession number: P0CT06 Secondary accession number(s): A4QU17 , G4N2R9, Q5EN15, Q8J232
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 18, 2013
	Last sequence update:	September 18, 2013
	Last modified:	November 7, 2018
	This is version 32 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0CT06 (ACEA_MAGO7)

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Isocitrate lyase

ICL1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glyoxylate cycle

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Peroxisome

Peroxisome

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: glyoxylate cycle

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ