ID ACEA_EMENI STANDARD; PRT; 537 AA. AC P28298; DT 01-DEC-1992 (Rel. 24, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN Name=acuD; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R153; RX MEDLINE=92136435; PubMed=1531185; RA Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.; RT "Characterization of the glyoxysomal isocitrate lyase genes of RT Aspergillus nidulans (acuD) and Neurospora crassa (acu-3)."; RL Curr. Genet. 21:43-47(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SEQUENCE REVISION TO 17 RP AND 156. RX MEDLINE=20264302; PubMed=10801489; DOI=10.1016/S0969-2126(00)00117-9; RA Britton K.L., Langridge S.J., Baker P.J., Weeradechapon K., RA Sedelnikova S.E., De Lucas J.R., Rice D.W., Turner G.; RT "The crystal structure and active site location of isocitrate lyase RT from the fungus aspergillus nidulans."; RL Structure 8:349-362(2000). CC -!- CATALYTIC ACTIVITY: Isocitrate = succinate + glyoxylate. CC -!- PATHWAY: Glyoxylate bypass; first step. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Glyoxysomal. CC -!- INDUCTION: By acetate. CC -!- SIMILARITY: Belongs to the isocitrate lyase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62696; CAA44572.1; ALT_SEQ. DR PDB; 1DQU; X-ray; A=1-536. DR InterPro; IPR006254; Isocit_lyase. DR InterPro; IPR000918; Isocit_lyase_ph. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase_ph; 1. DR TIGRFAMs; TIGR01346; isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. KW 3D-structure; Glyoxylate bypass; Glyoxysome; Lyase; KW Tricarboxylic acid cycle. FT ACT_SITE 205 205 SQ SEQUENCE 537 AA; 60193 MW; 7109E853C351962D CRC64; MSYIEEEDQR YWDEVAAVKN WWKDSRWRYT KRPFTAEQIV AKRGNLKIEY PSNVQAKKLW GILERNFNKE ASFTYGCLDP TMVTQMAKYL DTVYVSGWQS SSTASSTDEP SPDLADYPMN TVPNKVNHLW MAQLFHDRKQ REERMTTPKD QRHKVANVDY LRPIIADADT GHGGLTAVMK LTKLFVERGA AGIHIEDQAP GTKKCGHMAG KVLVPISEHI NRLVAIRAQA DIMGTDLLAI ARTDSEAATL ITSTIDHRDH PFIIGSTNPD IQPLNDLMVM AEQAGKNGAE LQAIEDEWLA KAGLKLFNDA VVDAINNSPL PNKKAAIEKY LTQSKGKSNL EARAIAKEIA GTDIYFDWEA PRTREGYYRY QGGTQCAINR AVAYAPFADL IWMESKLPDY KQAKEFADGV HAVWPEQKLA YNLSPSFNWK KAMPRDEQET YIKRLGALGY AWQFITLAGL HTTALISDTF AKAYAKQGMR AYGELVQEPE MANGVDVVTH QKWSGANYVD NMLKMITGGV SSTAAMGKGV TEDQFKS //