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Database: UniProt
Entry: B5JVN9_9GAMM
LinkDB: B5JVN9_9GAMM
Original site: B5JVN9_9GAMM 
ID   B5JVN9_9GAMM            Unreviewed;       534 AA.
AC   B5JVN9;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 63.
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:EDY86241.1};
GN   ORFNames=GP5015_1714 {ECO:0000313|EMBL:EDY86241.1};
OS   gamma proteobacterium HTCC5015.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY86241.1, ECO:0000313|Proteomes:UP000004692};
RN   [1] {ECO:0000313|Proteomes:UP000004692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX   PubMed=20472792; DOI=10.1128/JB.00510-10;
RA   Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequence of the novel marine member of the Gammaproteobacteria
RT   strain HTCC5015.";
RL   J. Bacteriol. 192:3838-3839(2010).
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; DS990604; EDY86241.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JVN9; -.
DR   STRING; 391615.GP5015_1714; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_038243_0_0_6; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000004692; Unassembled WGS sequence.
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:EDY86241.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004692}.
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ   SEQUENCE   534 AA;  59494 MW;  818CAF5FDA01FFD6 CRC64;
     MSQYLKDIEA MSKLVGAEGE RWNGINPESA ARMRAQNRFK TGLDIAQYTA DIMRKDMEEY
     DADSSKYTQS LGCWHGFVGQ QKLISIKKHF GTTDKRYLYL SGWMVAALRS EFGPLPDQSM
     HEKTSVPALI EELYTFLKQA DAWELNHLFR ELDAARDAGD SAKEKDIISK IDNFQTHVVP
     IIADIDAGFG NEEATYLLAK KMIEAGACAL QIENQVSDAK QCGHQDGKVT CPHVEFLSKI
     NALRYAFLEM GVENGVIVAR TDSLGAGLTQ KIAVSNEEGD LGSQYNSFID GDVIESAEDI
     GSNDVVIKQD GKLVRPKRLP SGLFQFKPGS GEDRVVLDCI TSLQNGADLL WIETEKPHVG
     QIAGMVNRIR EVVPNAKLVY NNSPSFNWTL NFRQQVFDAW TEEGKDVSSY DRDKLMSADY
     DETELGKVAD EWCQNFQRDA SREAGIFHHL ITLPTYHTVA LSTDNLAQGY FGEEGMLAYV
     AGVQRKEIRQ SIATVKHQDM AGSNIGDDHK EYFSKESALK AGGKDNTMGQ FENT
//
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