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Database: UniProt
Entry: A0A1H8FJV7_9MICO
LinkDB: A0A1H8FJV7_9MICO
Original site: A0A1H8FJV7_9MICO 
ID   A0A1H8FJV7_9MICO        Unreviewed;       538 AA.
AC   A0A1H8FJV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE   AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN   ORFNames=E3O10_03735 {ECO:0000313|EMBL:TFB93390.1};
OS   Cryobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1424661 {ECO:0000313|EMBL:TFB93390.1, ECO:0000313|Proteomes:UP000297654};
RN   [1] {ECO:0000313|EMBL:TFB93390.1, ECO:0000313|Proteomes:UP000297654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh15 {ECO:0000313|EMBL:TFB93390.1,
RC   ECO:0000313|Proteomes:UP000297654};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) 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:TFB93390.1}.
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DR   EMBL; SOFF01000012; TFB93390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8FJV7; -.
DR   STRING; 1424661.SAMN05216281_10665; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000297654; 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:TFB93390.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         101..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         380..384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   538 AA;  59579 MW;  07F9F6696EE2219D CRC64;
     MTAYQKDIED IEALKQQVGS SWDAINPESV ARMRAQNRFK TGLEIAQYTA DIMRKDMGEY
     DADSSVYTQS LGVWHGFIGQ QKMISIKKHL KTTNKRYLYL SGWMVAALRS EFGPLPDQSM
     HEKTTVPALV EEIYTFLRQA DARELDLLFT GLDNARIVGD DAKAAAIQTQ IDNFETHVVP
     IIADIDAGFG NPEATYLLAK KMIEAGACAI QIENQVSDEK QCGHQDGKVT VPHEDFIAKL
     NAVRYAFLEL GIENGIIVSR TDSLGAGLTQ KLAVTYTPGD LGDQYNSFLD VDEITEADLG
     NGDVVIKRDG KLLRPKRLAS NLFQFRAGTG EARCVLDSIT SLQNGADLLW IETEKPHIGQ
     IAAMMNEVRK EIPNAKLVYN NSPSFNWTLN FRQQAYDALL AEGKDVSAYD RAKLMSVDYD
     ETELALNADE KIRTFQRDSS KEAGIFHHLI TLPTYHTAAL STDDLAKGYF ADQGMLAYVK
     GVQRREIREG IATVKHQNMS GSDLGDNHKE YFAGAAALKA GGVNNTSNQF DEPALSSH
//
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