ACEA_HYPME
ID ACEA_HYPME Reviewed; 540 AA.
AC O50078;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:9395332};
DE Short=ICL {ECO:0000303|PubMed:9395332};
DE EC=4.1.3.1 {ECO:0000269|PubMed:9395332};
DE AltName: Full=Isocitrase {ECO:0000303|PubMed:9395332};
DE AltName: Full=Isocitratase {ECO:0000303|PubMed:9395332};
GN Name=aceA {ECO:0000250|UniProtKB:P0A9G6};
GN Synonyms=icl {ECO:0000303|PubMed:9395332};
OS Hyphomicrobium methylovorum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=84;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=GM2;
RX PubMed=9395332; DOI=10.1111/j.1432-1033.1997.t01-3-00820.x;
RA Tanaka Y., Yoshida T., Watanabe K., Izumi Y., Mitsunaga T.;
RT "Characterization, gene cloning and expression of isocitrate lyase involved
RT in the assimilation of one-carbon compounds in Hyphomicrobium methylovorum
RT GM2.";
RL Eur. J. Biochem. 249:820-825(1997).
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. May be
CC involved in the assimilation of one-carbon compounds via the isocitrate
CC lyase-positive serine pathway. {ECO:0000269|PubMed:9395332}.
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; Evidence={ECO:0000269|PubMed:9395332};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9395332};
CC Note=Can also use Mn(2+). {ECO:0000269|PubMed:9395332};
CC -!- ACTIVITY REGULATION: In the presence of magnesium, inhibited by
CC oxalate, potassium cyanide, manganese, silver, cadmium and to a lesser
CC extent by succinate, glycolate, iodoacetamide, DL-penicillamine,
CC aluminum, sodium, potassium, lithium and strontium.
CC {ECO:0000269|PubMed:9395332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 mM for D-isocitrate {ECO:0000269|PubMed:9395332};
CC pH dependence:
CC Optimum pH is 7.5. The enzyme is stable when incubated for 15 min at
CC 30 degrees Celsius at pH 7.5-9. {ECO:0000269|PubMed:9395332};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Loss of activity is 0%,
CC 16%, 30%, 82% and 100% when incubated at 25, 30, 40, 50 and 60
CC degrees Celsius for 30 min, respectively.
CC {ECO:0000269|PubMed:9395332};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000305|PubMed:9395332}.
CC -!- PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine
CC pathway. {ECO:0000305|PubMed:9395332}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9395332}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AB004651; BAA23678.1; -; Genomic_DNA.
DR AlphaFoldDB; O50078; -.
DR SMR; O50078; -.
DR UniPathway; UPA00703; UER00719.
DR UniPathway; UPA00927; -.
DR GO; GO:0004451; F:isocitrate lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; IDA:UniProtKB.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
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; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glyoxylate bypass; Lyase; Magnesium; Manganese;
KW Metal-binding; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9395332"
FT CHAIN 2..540
FT /note="Isocitrate lyase"
FT /evidence="ECO:0000269|PubMed:9395332"
FT /id="PRO_0000389621"
FT ACT_SITE 225
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 103..105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 226..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 385..389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 540 AA; 59898 MW; F289F07879534A7B CRC64;
MAHKKTYSQL RSELLARYPV GLTKGGVSID DIVQLRLQSP YESHLDVARA MASVMRADMA
AYDRDTGKFT QSLGCWSGFH AQQMIKAVKR LRGTTKGAYV YLSGWMVAGL RNRWGHLPDQ
SMHEKTSVVD LIEEIYVSLR QADEVALNDL FNELKDARAK GATNKACEEI ISRIDGFESH
VVPIIADIDA GFGNEHATYL LAKEMIKAGA CCLQIENQVS DAKQCGHQDG KVTVPREDFI
EKLRACRLAF EELGVDDGVI VARTDSLGAS LTQKIPVSQQ AGDFASSYIK WLKTEPITDA
NPLSEGELAI WQSGNFARPI RMPNGLFSFR EGTGRARVIE DCIASLKDGD ADLIWIETDT
PNVDEIASMV AEIRKQVPDA KLVYNNSPSF NWTLNLRKQV RAQWISEGKI AEADYPDGTA
LMSAQYDTSE LGREADDRLR QFQVDISARA GVFHNLITLP TFHLTAKSTD ELSHGYFGED
RMLAYVATVQ REEIRRSISA VRHQHEVGSD LGDTFKEMVS GDRALKAGGA HNTMNQFAAE
