ID N9KTS9_9GAMM Unreviewed; 533 AA.
AC N9KTS9; A0A2H9UKE9; A0A2H9YTC7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=CU320_10330 {ECO:0000313|EMBL:PJI32164.1}, CWI32_05965
GN {ECO:0000313|EMBL:PJO75916.1}, F906_00667
GN {ECO:0000313|EMBL:ENW87428.1};
OS Acinetobacter pseudolwoffii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=2053287 {ECO:0000313|EMBL:ENW87428.1, ECO:0000313|Proteomes:UP000023774};
RN [1] {ECO:0000313|EMBL:ENW87428.1, ECO:0000313|Proteomes:UP000023774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 713 {ECO:0000313|EMBL:ENW87428.1,
RC ECO:0000313|Proteomes:UP000023774};
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 sp. NIPH 713.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PJO75916.1, ECO:0000313|Proteomes:UP000243446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 5044 {ECO:0000313|EMBL:PJO75916.1,
RC ECO:0000313|Proteomes:UP000243446};
RA Nemec A., Radolfova-Krizova L.;
RT "Revising the taxonomy of the Acinetobacter lwoffii group: the description
RT of Acinetobacter pseudolwoffii sp. nov. and emended description of
RT Acinetobacter lwoffii.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PJI32164.1, ECO:0000313|Proteomes:UP000242351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 5347 {ECO:0000313|EMBL:PJI32164.1,
RC ECO:0000313|Proteomes:UP000242351};
RA Han C.G.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PJI32164.1, ECO:0000313|Proteomes:UP000242351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 5347 {ECO:0000313|EMBL:PJI32164.1,
RC ECO:0000313|Proteomes:UP000242351};
RA Nemec A.;
RT "Revising the taxonomy of the Acinetobacter lwoffii group: the description
RT of Acinetobacter pseudolwoffii sp. nov. and emended description of
RT Acinetobacter lwoffii.";
RL Submitted (DEC-2017) 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:ENW87428.1}.
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DR EMBL; APRJ01000010; ENW87428.1; -; Genomic_DNA.
DR EMBL; PGOZ01000012; PJI32164.1; -; Genomic_DNA.
DR EMBL; PHRG01000002; PJO75916.1; -; Genomic_DNA.
DR RefSeq; WP_005169883.1; NZ_PHRG01000002.1.
DR AlphaFoldDB; N9KTS9; -.
DR GeneID; 83722886; -.
DR PATRIC; fig|1217709.3.peg.630; -.
DR HOGENOM; CLU_038243_0_0_6; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000023774; Unassembled WGS sequence.
DR Proteomes; UP000242351; Unassembled WGS sequence.
DR Proteomes; UP000243446; 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:ENW87428.1};
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; 59078 MW; B043E9477763B6F9 CRC64;
MTTYQTAIDA IRELKAKFGN TWADISPEDA ARMQIQNRFK TGLDIAKYTA AIMRRDMAAY
DADSSKYTQS LGCWHGFIAQ QKMIANKKYF GTTERRYIYL SGWMVAALRS EFGPLPDQSM
HEKTSVPALI EEIYTFLRQA DAKELNDLFR ALKKAQEAGD TAKAAELTSQ IDNFQTHVVP
IIADIDAGFG NEEATYLLAK KMIEAGACAL QIENQVSDAK QCGHQAGKVT VPHEDFIAKI
HALRYAFLEM GLDDGIIVAR TDSEGADLTQ KIPVVKEPGD IASQYISYLE TSEIDIADAQ
EDEILIKRDG KLHRPKRLAS GLYQFREGTQ IDRVVLDCVT SLQNGADLLW IETATPNVAE
IAHMVNRVKE TVPNAKLVYN NSPSFNWTLN FRQQAYDRWV AEGKDVSAYD RAKLMSAEYD
ATELAAEADE KVRTFQADAA REAGVFHHLI TLPTYHTAAL STHELAQGYF GSEGMLAYVA
GVQRKEIRGG IACVKHQAMA GSDIGDDHKE IFAGDNALKA GDDAKNTMNQ FSA
//
