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Database: UniProt
Entry: A0A0N1BHC1_9SPHN
LinkDB: A0A0N1BHC1_9SPHN
Original site: A0A0N1BHC1_9SPHN 
ID   A0A0N1BHC1_9SPHN        Unreviewed;       530 AA.
AC   A0A0N1BHC1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=IP68_05230 {ECO:0000313|EMBL:KPF75922.1};
OS   Blastomonas sp. AAP25.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Blastomonas.
OX   NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF75922.1, ECO:0000313|Proteomes:UP000037930};
RN   [1] {ECO:0000313|EMBL:KPF75922.1, ECO:0000313|Proteomes:UP000037930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP25 {ECO:0000313|EMBL:KPF75922.1,
RC   ECO:0000313|Proteomes:UP000037930};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF75922.1}.
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DR   EMBL; LJHP01000005; KPF75922.1; -; Genomic_DNA.
DR   RefSeq; WP_054133920.1; NZ_LJHP01000005.1.
DR   AlphaFoldDB; A0A0N1BHC1; -.
DR   PATRIC; fig|1523416.3.peg.3073; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000037930; 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:KPF75922.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037930}.
FT   ACT_SITE        221
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         100..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         222..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         379..383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         450
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   530 AA;  58935 MW;  714125F70FB662E0 CRC64;
     MPYTDQIRAN EQLIGSKQGR WTGIDAESVA RMQLQNRFRT GLDIARYTAK IMREDMAAYD
     ADSSQYTQSL GCWHGFIAQQ KMISIKKHFG TTKRKYLYLS GWMVAALRSD FGPLPDQSMH
     EKTSVPALIE ELYTFLRQAD ARELDLLFTG IDKARAAGDS AKEKELLAQV DNFQTHVVPI
     IADIDAGFGN AEATYLLAKK MIEAGACALQ IENQVSDEKQ CGHQDGKVTV PHEDFLAKIR
     ACRYAFLELG VEDGIIVTRT DSLGAGLTKQ IAVSNEPGDL GDQYNSFLDC EEIDPATARN
     GDVIINRNGK LLRPKRLPSN LFQFREGTGE DRCVLDSITS LQNGADLLWI ETEKPHVEQI
     AGMMDRVREV IPNAKLVYNN SPSFNWTLNF RQQVYDAMVS EGLDVSEYDR AQLMDAKYDD
     TELGIAADKR IRTFQADGAK RAGIFHHLIT LPTYHTAALS TDNLAKEYFG EAGMLGYVLG
     VQRQELRQGI ACVKHQNMSG SDIGDAHKEY FAGEAALKAG GVNNTMNQFG
//
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