ID V4P9M9_9CAUL Unreviewed; 426 AA.
AC V4P9M9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=AEAC466_06785 {ECO:0000313|EMBL:ESQ84756.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ84756.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ84756.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ84756.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ84756.1}.
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DR EMBL; AWGE01000006; ESQ84756.1; -; Genomic_DNA.
DR RefSeq; WP_023457388.1; NZ_AWGE01000006.1.
DR AlphaFoldDB; V4P9M9; -.
DR STRING; 1282362.AEAC466_06785; -.
DR PATRIC; fig|1282362.3.peg.1361; -.
DR eggNOG; COG2224; Bacteria.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000017826; 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:ESQ84756.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000017826}.
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 308..312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 426 AA; 47183 MW; EFEA8968A86A57E6 CRC64;
MTTFQDLVPT AAPDRFDGIE RPYTPADVLR LRGSFPIQHT LAERGANRLW DLLHTEPFIN
SLGAMTGNQA MQMVRAGLKA IYLSGWQVAA DSNTASSMYP DQSLYPANAA PELCRRINRT
LQRADQIEHS EGGAKREWFA PIVADAEAGF GGPLNSFEIM KAFIEAGAAG VHFEDQLASE
KKCGHLGGKV LIPTQAHERN LISARLAADV MGVPTLTVAR TDAESAQLIT SDVDERDHPF
IERDNRTVEG FFRLKPGTGL DHCIARGLSY ARYADLLWWE TSHPDLDDAR RFAEAVHKQY
PGKLLAYNCS PSFNWEAKLD KATIAKFQRE LGAMGYKYQF VTLAGFHALN NSMFELADGY
RDHGMAAYSE LQQREFANEA RGYTATRHQR EVGTGYFDKI AETITNGQSS TTAMKASTET
AQFAAE
//
