ACEA_COCIM
ID ACEA_COCIM Reviewed; 538 AA.
AC Q96TP5; J3KKS8; Q1E625;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE Short=ICL {ECO:0000305};
DE Short=Isocitrase {ECO:0000305};
DE Short=Isocitratase {ECO:0000305};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Methylisocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE Short=MICA {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN Name=ICL1 {ECO:0000250|UniProtKB:P28240}; ORFNames=CIMG_01988;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Shi Q., Ivey F.D., Woitaske M.D., Magee D.M., Cox R.A.;
RT "Cloning of isocitrate lyase of Coccidioides immitis.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle.
CC Required for growth on ethanol or acetate, but dispensable when
CC fermentable carbon sources are available. Acts also on 2-
CC methylisocitrate. {ECO:0000250|UniProtKB:P28240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000250|UniProtKB:P28240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000250|UniProtKB:P28240};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28240}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AF420484; AAL16915.1; -; Genomic_DNA.
DR EMBL; AY038602; AAK72548.2; -; mRNA.
DR EMBL; GG704911; EAS36634.3; -; Genomic_DNA.
DR RefSeq; XP_001248217.1; XM_001248216.2.
DR AlphaFoldDB; Q96TP5; -.
DR SMR; Q96TP5; -.
DR STRING; 246410.Q96TP5; -.
DR PRIDE; Q96TP5; -.
DR EnsemblFungi; EAS36634; EAS36634; CIMG_01988.
DR GeneID; 4567087; -.
DR KEGG; cim:CIMG_01988; -.
DR VEuPathDB; FungiDB:CIMG_01988; -.
DR InParanoid; Q96TP5; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 905115at2759; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 2: Evidence at transcript level;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..538
FT /note="Isocitrate lyase"
FT /id="PRO_0000068788"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 98..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 208..209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 424..428
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 272
FT /note="N -> T (in Ref. 1; AAK72548/AAL16915)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..329
FT /note="AI -> TT (in Ref. 1; AAK72548/AAL16915)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="V -> I (in Ref. 1; AAK72548/AAL16915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60383 MW; CD722C99DB39502C CRC64;
MSLSVEQEEQ KYWEEVEAVK QWWKDSRWRY TKRPFTAEQI VAKRGNLKIE YPSNVQSKKL
WKLVEEKFKT KTASFTYGCL DPTMVTQMVK YLDTVYVSGW QSSSTASSTD EPSPDLADYP
MNTVPNKVNQ LWMAQLFHDR KQREERLRNP KEKRASLANI DYLAPIIADA DTGHGGLTAV
MKLTKLFIER GAAGIHIEDQ APGTKKCGHM AGKVLVPISE HINRLVAIRA QADIMGTDLL
AIARTDSEAA TLITSTIDPR DHAFVVGSTN PNLEPLNDLM IAAERAGKNG AELQAIEDSW
TAKAGLKRFE DAVIDQIKAS SAANKQAAID AFLREIKGKS NKEARAIARQ ILGTDIFWDW
DAPRTREGYY RYQGGCQCAI NRAVAFAPFA DLIWMESKLP DYAQAKEFAE GVHAVWPQQK
LAYNLSPSFN WKAAMPRDEQ ETYIRRLGEL GYCWQFITLA GLHTTALISD QFAKAYAKQG
MRAYGELVQE PEMENKVDVV THQKWSGANY VDELLKMVTG GVSSTSAMGK GVTEDQFK
