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
//