ACEB_SCHPO
ID ACEB_SCHPO Reviewed; 518 AA.
AC Q9P6J1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Mitochondrial 2-methylisocitrate lyase;
DE Short=Methylisocitrate lyase;
DE EC=4.1.3.30;
GN Name=icl2; ORFNames=SPBC1683.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB91173.1; -; Genomic_DNA.
DR RefSeq; NP_595067.1; NM_001020973.2.
DR AlphaFoldDB; Q9P6J1; -.
DR SMR; Q9P6J1; -.
DR STRING; 4896.SPBC1683.11c.1; -.
DR MaxQB; Q9P6J1; -.
DR PaxDb; Q9P6J1; -.
DR EnsemblFungi; SPBC1683.11c.1; SPBC1683.11c.1:pep; SPBC1683.11c.
DR GeneID; 2539803; -.
DR KEGG; spo:SPBC1683.11c; -.
DR PomBase; SPBC1683.11c; -.
DR VEuPathDB; FungiDB:SPBC1683.11c; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; Q9P6J1; -.
DR OMA; GMDHADY; -.
DR PhylomeDB; Q9P6J1; -.
DR UniPathway; UPA00946; -.
DR PRO; PR:Q9P6J1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
DR GO; GO:0046421; F:methylisocitrate lyase activity; ISS:PomBase.
DR GO; GO:0006567; P:threonine catabolic process; ISS:PomBase.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Mitochondrion; Reference proteome.
FT CHAIN 1..518
FT /note="Mitochondrial 2-methylisocitrate lyase"
FT /id="PRO_0000314754"
SQ SEQUENCE 518 AA; 58938 MW; E446878F9AF259E5 CRC64;
MTTDMDLEQL EYEKEVEEIE KWWATPKQSQ IKRPYTASTV AVLSEVTKAY YPSSQQALKL
YDLLREHRNK GTATLTYGVV DPVLASQASK AGLETIFVSG CLCGLSSVDE PGMDHADYPW
DTVPKAVDRI FRSQNWHARR QKQFHLMKPA EERKQLPKYD YLLPIIADGD MGFGSVTSTM
KMTKRFVESG VAMIHLDDLA IGLKRFTVGQ GRTVVPTSEY LRRLTAVRLQ FDIMKAETML
LCRCDTDHAE FITSVVDPRD HAYVLGATTK IESLIKALKD AESTGVSMKK ARENWIERAK
LMTFDEAVKS TATPKEYENY ISAISKKPFH SISERQELAE KYLSNEVFFD WELPRSSDGQ
YFFKPTVQTV IERAIAAAPL GEMTWARMDY PKWQDIKAFH EGVRAVYPDR MFAFGFTGNY
DFKAAGFSEE QLRNLTSDMA KLGVCWQVQP YFTCQVLNKA SVDYSNIWKK DGIFGYVKTV
QEPALKEDVD GFENEWCGTY FADKLLSAAG SSDKTIPY
