ACEB_EMENI
ID ACEB_EMENI Reviewed; 610 AA.
AC C8V9Y5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Methylisocitrate lyase, mitochondrial;
DE EC=4.1.3.30;
DE AltName: Full=2-methylisocitrate lyase, mitochondrial;
DE Flags: Precursor;
GN Name=mclA; ORFNames=AN8755;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP PROTEIN SEQUENCE OF 41-51, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16151139; DOI=10.1128/aem.71.9.5465-5475.2005;
RA Brock M.;
RT "Generation and phenotypic characterization of Aspergillus nidulans
RT methylisocitrate lyase deletion mutants: methylisocitrate inhibits growth
RT and conidiation.";
RL Appl. Environ. Microbiol. 71:5465-5475(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=11422389; DOI=10.1046/j.1432-1327.2001.02262.x;
RA Brock M., Darley D., Textor S., Buckel W.;
RT "2-Methylisocitrate lyases from the bacterium Escherichia coli and the
RT filamentous fungus Aspergillus nidulans: characterization and comparison of
RT both enzymes.";
RL Eur. J. Biochem. 268:3577-3586(2001).
CC -!- FUNCTION: Catalyzes the formation of pyruvate and succinate from 2-
CC methylisocitrate during the metabolism of endogenous propionyl-CoA.
CC {ECO:0000269|PubMed:11422389, ECO:0000269|PubMed:16151139}.
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:11422389, ECO:0000269|PubMed:16151139};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11422389};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58 uM for magnesium {ECO:0000269|PubMed:11422389,
CC ECO:0000269|PubMed:16151139};
CC KM=3.33 mM for methylisocitrate {ECO:0000269|PubMed:11422389,
CC ECO:0000269|PubMed:16151139};
CC KM=0.35 mM for isocitrate {ECO:0000269|PubMed:11422389,
CC ECO:0000269|PubMed:16151139};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth with propionate as the sole carbon
CC and energy source. {ECO:0000269|PubMed:16151139}.
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; BN001303; CBF78090.1; -; Genomic_DNA.
DR AlphaFoldDB; C8V9Y5; -.
DR SMR; C8V9Y5; -.
DR STRING; 162425.CADANIAP00006310; -.
DR EnsemblFungi; CBF78090; CBF78090; ANIA_08755.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; C8V9Y5; -.
DR OMA; ARFQWDM; -.
DR OrthoDB; 905115at2759; -.
DR SABIO-RK; C8V9Y5; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000560; Chromosome III.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
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 Direct protein sequencing; Lyase; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:16151139"
FT CHAIN 41..610
FT /note="Methylisocitrate lyase, mitochondrial"
FT /id="PRO_0000428796"
FT REGION 588..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10119"
SQ SEQUENCE 610 AA; 67596 MW; 0BE355E9421BCD32 CRC64;
MLRSIPRRVP RRLPIFTTTA TAGGPSRLAQ RAFTCGYLRM SPSSLPPVQP PVSSTLPSDS
YQLLSTADKA GDAEDALYEQ QIKDVEAWWN SPRFEGIKRP YSAADVVSKR GSLQQTYPSS
LMARKLFNLL NERAAENKPV HTMGAIDPVQ MTQQAPNQEV LYVSGWACSS VLTTTNEVSP
DFGDYPYNTV PNQVQRLFKA QQLHDRKHWD ARRKMTPEQR KSTPYIDYMR PIIADGDTGH
GGLTAVLKLA KLFAENGAAA VHFEDQMHGG KKCGHLAGKV LVPIGEHINR LVATRFQWDM
MGVENLVIAR TDSESGKLLS SAIDVRDHEF ILGVTEESEP LAETLQAMER EGAAPSEIDA
FELDWVKRHK LVTFDEAVDA HLEAEGAPQA ARDAYKKRVK ENPDLSITRR RELANDYTKT
PVVWSCDIPR TREGFYHYRA GFPAATKRAK EFGPYADLLW VETGDPNVEK AAKLAGEVRA
ALPGKKLVYN LSPSFNWMGQ GFDEASLKSF IWDLAQHGFV LQLISLAGLH SGATITAELS
RAFKDEGMLA YVRLIQAREK ELGVDVLTHQ KWSGAPYMDG IVGAIQSGSS SSKSMGEGNT
EKGEFNPLVF
