ACEA_COREF
ID ACEA_COREF Reviewed; 431 AA.
AC Q8RQN6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P42449};
DE Short=ICL {ECO:0000250|UniProtKB:P42449};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P42449};
DE AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P42449};
DE AltName: Full=Isocitratase {ECO:0000250|UniProtKB:P42449};
GN Name=aceA; OrderedLocusNames=CE2232;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA Hirano S., Kimura E., Kawahara Y., Sugimoto S.;
RT "aceA of Corynebacterium efficiens.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
CC -!- FUNCTION: Involved in the metabolic adaptation in response to
CC environmental changes. Catalyzes the reversible formation of succinate
CC and glyoxylate from isocitrate, a key step of the glyoxylate cycle,
CC which operates as an anaplerotic route for replenishing the
CC tricarboxylic acid cycle during growth on fatty acid substrates.
CC {ECO:0000250|UniProtKB:P42449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000250|UniProtKB:P42449};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P42449};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000250|UniProtKB:P42449}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P42449}.
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; AB083050; BAB88666.1; -; Genomic_DNA.
DR EMBL; BA000035; BAC19042.1; -; Genomic_DNA.
DR RefSeq; WP_006768237.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8RQN6; -.
DR SMR; Q8RQN6; -.
DR STRING; 196164.23494074; -.
DR PRIDE; Q8RQN6; -.
DR EnsemblBacteria; BAC19042; BAC19042; BAC19042.
DR KEGG; cef:CE2232; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_019214_2_0_11; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 152545at2; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001409; Chromosome.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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; 2.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 2.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..431
FT /note="Isocitrate lyase"
FT /id="PRO_0000068772"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 315..319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 428
FT /note="G -> C (in Ref. 1; BAB88666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47031 MW; A6ACDA9530A6B207 CRC64;
MSNVGTPRTA QEIQQDWDTN PRWNGITRDY TAEQVAELQG SVVEEHTLAK RGAEILWDAV
SAEGDDYINA LGALTGNQAV QQVRAGLKAV YLSGWQVAGD ANLAGHTYPD QSLYPANSVP
NVVRRINNAL LRADEIARVE GDTSVDNWLV PIVADGEAGF GGALNVYELQ KGMITAGAAG
THWEDQLASE KKCGHLGGKV LIPTQQHIRT LNSARLAADV ANTPTVVIAR TDAEAATLIT
SDVDERDRPF ITGERTAEGY YHVKPGLEPC IARAKSYAPY ADMIWMETGT PDLELAKKFA
EGVRSEFPDQ LLSYNCSPSF NWSAHLEADE IAKFQKELGA MGFKFQFITL AGFHSLNYGM
FDLAYGYARE GMPAFVDLQN REFKAAEERG FTAVKHQREV GAGYFDTIAT TVDPNSSTTA
LKGSTEEGQF H
