ID N9CSA5_9GAMM Unreviewed; 533 AA.
AC N9CSA5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=F947_00032 {ECO:0000313|EMBL:ENV71098.1};
OS Acinetobacter towneri DSM 14962 = CIP 107472.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120929 {ECO:0000313|EMBL:ENV71098.1, ECO:0000313|Proteomes:UP000023781};
RN [1] {ECO:0000313|EMBL:ENV71098.1, ECO:0000313|Proteomes:UP000023781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107472 {ECO:0000313|EMBL:ENV71098.1,
RC ECO:0000313|Proteomes:UP000023781};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter towneri CIP 107472.";
RL Submitted (FEB-2013) 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:ENV71098.1}.
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DR EMBL; APPY01000008; ENV71098.1; -; Genomic_DNA.
DR RefSeq; WP_004977281.1; NZ_KB849699.1.
DR AlphaFoldDB; N9CSA5; -.
DR PATRIC; fig|1120929.3.peg.24; -.
DR HOGENOM; CLU_038243_0_0_6; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000023781; 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:ENV71098.1};
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 533 AA; 59311 MW; 6D0FD0FCA7B7BBB8 CRC64;
MTTYQTAIDA IRELKAKFGN TWADISPEDA ARMQMQNRFK TGLDIAKYTA AIMRRDMAAY
DADSSKYTQS LGCWHGFVAQ QKMIANKKYF GTTERRYIYL SGWMVAALRS EFGPLPDQSM
HEKTSVPALI EEIYTFLRQA DAKELNDLFR ALKKAQDAGD TAKAAEITAQ IDNFETHVVP
IIADIDAGFG NEEATYLLAK KMIEAGACAL QIENQVSDAK QCGHQAGKVT VPHEDFIAKI
HALRYAFLEM GLDDGIIVAR TDSEGADLTQ KIPVVKEPGD IASQYISYLD TQEIDISEAK
EDEILIKRDG KLHRPKRLAS GLYQFREGTQ IDRVVLDCVT SLQNGADLLW IETATPNVEE
IAHMVNRVRE VVPNAKLVYN NSPSFNWTLN FRQQAYDRWV AEGKDVSAYD RAKLMSAEYD
DSELAAEADE KVRTFQADAS REAGVFHHLI TLPTYHTAAL STHELAQGYF GSEGMLAYVA
GVQRKEIRGG IACVKHQAMA GSDIGDDHKE IFSGDNALKA ADEAKNTMNQ FNA
//
