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Database: UniProt
Entry: A4AG98_9ACTN
LinkDB: A4AG98_9ACTN
Original site: A4AG98_9ACTN 
ID   A4AG98_9ACTN            Unreviewed;       433 AA.
AC   A4AG98;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
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   ORFNames=A20C1_03881 {ECO:0000313|EMBL:EAR25373.1};
OS   marine actinobacterium PHSC20C1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25373.1, ECO:0000313|Proteomes:UP000003868};
RN   [1] {ECO:0000313|EMBL:EAR25373.1, ECO:0000313|Proteomes:UP000003868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25373.1,
RC   ECO:0000313|Proteomes:UP000003868};
RA   Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR25373.1}.
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DR   EMBL; AAOB01000003; EAR25373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4AG98; -.
DR   STRING; 312284.A20C1_03881; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_2_0_11; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000003868; 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; 1.
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:EAR25373.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         96..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         318..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   433 AA;  47464 MW;  3E48ECF3C89CB388 CRC64;
     MTSNRPGDQN QTAAELETEW KTDARWNGVE RDFSAEDVIA LRGSVREDRT LARRGAENLW
     NLIQRDDTEW VAALGALTGN QAVQQVRAGL EAIYLSGWQV AADANLSGQT YPDQSLYPAN
     SVPAVVRRIN NALLRADQIE TAESGAPSTD WMAPIVADAE AGFGGPLNAY ELMSSMIEAG
     AAGVHWEDQL ASEKKCGHMG GKVLIPTAQH VRTLNAARLA ADVAGVSSII IARTDSLAAD
     LITNDVDDRD KPFLTGERTS DGFYRTTPGI ETVLSRGHAY APYADLLWVE SAKPDLELAR
     TFAESIHKEF PGKKLAYNCS PSFNWKRHLD DAQIATFQRE LAAMGYAFQF ITLAGFHALN
     HSMYTLARDY NERHMSAYVE LQEAEFASEN DGYTATRHQR EVGTGYFDRI ATALNPASET
     LALVGSTETA QFH
//
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