ID S5TWP2_9GAMM Unreviewed; 532 AA.
AC S5TWP2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN Name=aceA {ECO:0000313|EMBL:AGS39590.1};
GN ORFNames=CYCME_1261 {ECO:0000313|EMBL:AGS39590.1};
OS Cycloclasticus zancles 78-ME.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1198232 {ECO:0000313|EMBL:AGS39590.1, ECO:0000313|Proteomes:UP000015380};
RN [1] {ECO:0000313|EMBL:AGS39590.1, ECO:0000313|Proteomes:UP000015380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-ME {ECO:0000313|Proteomes:UP000015380};
RA Yakimov M.M., Messina E., Genovese M., Denaro R., Crisafi F., Russo D.,
RA Cappello S., Santisi S., Smedile F., Golyshina O.V., Tran H., Pieper D.H.,
RA Golyshin P.N., Giuliano L.;
RT "Between feast and famine: a lifestyle of most important marine PAH-
RT degrading bacterium Cycloclasticus sp. 7ME.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023531};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
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DR EMBL; CP005996; AGS39590.1; -; Genomic_DNA.
DR RefSeq; WP_015005973.1; NC_021917.1.
DR AlphaFoldDB; S5TWP2; -.
DR KEGG; cza:CYCME_1261; -.
DR PATRIC; fig|1198232.3.peg.1261; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_038243_0_0_6; -.
DR Proteomes; UP000015380; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AGS39590.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 224..225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 381..385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 532 AA; 59033 MW; 1371F5F67425F618 CRC64;
MSSYTNDINA VSELVQAKGD SWAAINPESV ARMRAQNKFK TGLDIAQYTA DIMNADMAAF
DADNTLYTQS LGCWHGFIGQ QKMISIKKHF GGKTDRRYLY LSGWMVAALR SEFGPLPDQS
MHEKTAVASL VEELYTFLRQ ADARELGGLF RQLDTAREAG DEATVEQIQE EIDNHVTHVV
PIVADIDAGF GNAEATYLMA KQMIEAGACC LQIENQVADE KQCGHQDGKV TVPHADFHAK
IRALRHAFLE LGIDNGLIVA RTDSEGAGLT KEIAVVKEPG DQGDQYNSFL DVEEIDVADM
AEGDVCFNRD GKLVRPKRLP SGLYQFRQGT GPERCVFDSI EAIKAGADLL WIETATPSVK
DIADMMNEVR KEIPNAKLVY NNSPSFNWTL NFRQQAYDRW VEEGKDVSAY DREDLMNAKY
DATELAADAD DKIRTFQADS SREANIFHHL ITLPTYHTAA LSTDNLAKEY FGEAGMLGYV
RDVQRKEIRQ GIACVKHQNM SGSDMGDDHK EYFAGENALK AGGAKNTSNQ FS
//
