ACEB_YEAST
ID ACEB_YEAST Reviewed; 575 AA.
AC Q12031; D6W417;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial 2-methylisocitrate lyase ICL2 {ECO:0000303|PubMed:11092862};
DE Short=Methylisocitrate lyase;
DE EC=4.1.3.30 {ECO:0000269|PubMed:11092862};
GN Name=ICL2; OrderedLocusNames=YPR006C; ORFNames=LPZ6C, YP9723.06C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=8923733;
RX DOI=10.1002/(sici)1097-0061(199610)12:13<1285::aid-yea5>3.0.co;2-b;
RA Heinisch J.J., Valdes E., Alvarez J., Rodicio R.;
RT "Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in
RT Saccharomyces cerevisiae.";
RL Yeast 12:1285-1295(1996).
RN [4]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=11092862; DOI=10.1128/jb.182.24.7007-7013.2000;
RA Luttik M.A.H., Koetter P., Salomons F.A., van der Klei I.J.,
RA van Dijken J.P., Pronk J.T.;
RT "The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-
RT methylisocitrate lyase involved in propionyl-coenzyme A metabolism.";
RL J. Bacteriol. 182:7007-7013(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Catalyzes the formation of pyruvate and succinate from 2-
CC methylisocitrate during the metabolism of endogenous propionyl-CoA.
CC Does not act on isocitrate. {ECO:0000269|PubMed:11092862}.
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:0000269|PubMed:11092862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16810;
CC Evidence={ECO:0000305|PubMed:11092862};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11092862, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- INDUCTION: Repressed by glucose and induced by ethanol and threonine.
CC {ECO:0000269|PubMed:11092862, ECO:0000269|PubMed:8923733}.
CC -!- MISCELLANEOUS: Present with 1084 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; Z71255; CAA95046.1; -; Genomic_DNA.
DR EMBL; Z48951; CAA88784.1; -; Genomic_DNA.
DR EMBL; U31900; AAA97585.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11433.1; -; Genomic_DNA.
DR PIR; S52819; S52819.
DR RefSeq; NP_015331.1; NM_001184103.1.
DR AlphaFoldDB; Q12031; -.
DR SMR; Q12031; -.
DR BioGRID; 36183; 46.
DR DIP; DIP-4593N; -.
DR IntAct; Q12031; 1.
DR STRING; 4932.YPR006C; -.
DR PaxDb; Q12031; -.
DR PRIDE; Q12031; -.
DR EnsemblFungi; YPR006C_mRNA; YPR006C; YPR006C.
DR GeneID; 856114; -.
DR KEGG; sce:YPR006C; -.
DR SGD; S000006210; ICL2.
DR VEuPathDB; FungiDB:YPR006C; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; Q12031; -.
DR OMA; ARFQWDM; -.
DR BioCyc; YEAST:G3O-34168-MON; -.
DR UniPathway; UPA00946; -.
DR PRO; PR:Q12031; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12031; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IDA:SGD.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:SGD.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
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 1: Evidence at protein level;
KW Lyase; Mitochondrion; Reference proteome.
FT CHAIN 1..575
FT /note="Mitochondrial 2-methylisocitrate lyase ICL2"
FT /id="PRO_0000068800"
FT ACT_SITE 238
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64976 MW; C29A9A62A02BD291 CRC64;
MITMINNKTF NRKTTGTLKK LVLSSDKSLR RSFNGASSTK DFVFSESSKV EEWWESARFK
NISRPYSATD VVKHRGSLPA NTSIYPSSYQ ARKLFNLLEE NFKNGTPLHT LGVIDPVQMS
QLARCRNIKV AYISGWACSS TLVGSTNEVS PDFGDYPYDT VPNQVERIFK AQQLHDRKAF
LEASIKGSTP VDYLKPIIAD ADMGHGGPTT VMKVAKLFAE KGAAGIHLED QMVGGKRCGH
LSGAVLVPTA THLMRLISTR FQWDIMGTEN LVIARTDSCN GKLLSSSSDP RDHEFIRGII
RDNVVPWSEK LIEMEDKKIP NSAIADMEKE WYHENELFTF EEALEKQFTA SEFESYKEKK
EDLMVNKLGR AYLSLREMKL LAQEVTPLKK IIFDWDAPRT KEGYYMFNGC IEAAIRRSLV
FAPYSDMIWL ETKTPDLEQA RSFSRKIHKQ LPATKLVYNL SPSFNWSAHG FDDKALKSFV
WDLAKEGFTL QLVSLAGLHS DGVSFWELAN SFQSDGMKAY VEKVQKREKE TNCDIMTHQL
WSGAEYVDSL MKVVQNGASS QTLSTSGESF TETQF
