ID A2QV31_ASPNC Unreviewed; 299 AA.
AC A2QV31;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Contig An10c0050, genomic contig {ECO:0000313|EMBL:CAK40518.1};
DE EC=2.7.8.23 {ECO:0000313|EMBL:CAK40518.1};
GN ORFNames=An10g00820 {ECO:0000313|EMBL:CAK40518.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40518.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK40518.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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:0000256|ARBA:ARBA00001050};
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DR EMBL; AM270216; CAK40518.1; -; Genomic_DNA.
DR RefSeq; XP_001402473.2; XM_001402436.2.
DR AlphaFoldDB; A2QV31; -.
DR SMR; A2QV31; -.
DR EnsemblFungi; CAK40518; CAK40518; An10g00820.
DR GeneID; 4990333; -.
DR HOGENOM; CLU_027389_3_0_1; -.
DR Proteomes; UP000006706; Chromosome 5EL.
DR GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:RHEA.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
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; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF2; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000313|EMBL:CAK40518.1}.
SQ SEQUENCE 299 AA; 32422 MW; ED85E5F43736C253 CRC64;
MVTGASKLRK QLRETNELLV CPGVYDGLSA RIAINLGFKG MYMTGAGTTA SRLGMADLGL
AHIYDMKTNA EMIANLDPYG PPLIADMDTG YGGPLMVARS VQQYIQAGVA GFHIEDQIQN
KRCGHLAGKR VVTMDEYLTR IRAAKLTKDR LRSDIVLIAR TDALQQHGYD ECIRRLKAAR
DLGADVGLLE GFTSKEMARR CVQDLAPWPL LLNMVENGAG PVISVDEARE MGFRIMIFSF
ACITPAYMGI TAALERLKKD GVVGLPEGMG PKKLFEVCGL MDSVRVDTEA GGDGFANGV
//
