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Database: UniProt
Entry: B8LA53_9GAMM
LinkDB: B8LA53_9GAMM
Original site: B8LA53_9GAMM 
ID   B8LA53_9GAMM            Unreviewed;       433 AA.
AC   B8LA53;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE            EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
DE   AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE   AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN   Name=aceA {ECO:0000313|EMBL:EED40201.1};
GN   ORFNames=SSKA14_3220 {ECO:0000313|EMBL:EED40201.1};
OS   Stenotrophomonas sp. SKA14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=391601 {ECO:0000313|EMBL:EED40201.1};
RN   [1] {ECO:0000313|EMBL:EED40201.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA14 {ECO:0000313|EMBL:EED40201.1};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (DEC-2008) 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; DS999412; EED40201.1; -; Genomic_DNA.
DR   RefSeq; WP_004153647.1; NZ_DS999412.1.
DR   AlphaFoldDB; B8LA53; -.
DR   HOGENOM; CLU_019214_2_0_6; -.
DR   Proteomes; UP000003991; 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; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01346; isocit_lyase; 2.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 2.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EED40201.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   REGION          409..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         88..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         309..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   433 AA;  47399 MW;  A808FD83251681FC CRC64;
     MSKLPTAEQI QHDWDTNPRW EGIQRNYSAA DVVRLRGTVH IEHSLARLGA EKLWASLHER
     EFVNALGALT GNQAMQQVKA GLKAIYLSGW QVAADANLAG QMYPDQSLYP ADSVPAVVKR
     INNTLLRADQ LHHAEGKDDI DFLQPIVADA EAGFGGVLNA FELMKAMIEA GAAGVHFEDQ
     LASVKKCGHM GGKVLVPTRE AIEKLNAARL AADVLGVPTL LVARTDAEAA DLLTSDIDGN
     DKPFATGERT VEGFYKTRNG LDQAISRGLA YAPYADLVWC ETGKPDLEFA RKFAEAIHAK
     FPGKLLAYNC SPSFNWKKNL DDATIAKFQR ELGSYGYKFQ FITLAGFHAL NYGMFNLAHG
     YARRQMSAFV ELQEAEFEAA ERGFTAVKHQ REVGTGYFDA VTQAIQQGQS STTALTGSTE
     EEQFHGGRSE RAA
//
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