ID N8RFB1_9GAMM Unreviewed; 534 AA.
AC N8RFB1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=F989_01046 {ECO:0000313|EMBL:ENU34073.1};
OS Acinetobacter parvus NIPH 1103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217671 {ECO:0000313|EMBL:ENU34073.1, ECO:0000313|Proteomes:UP000018426};
RN [1] {ECO:0000313|EMBL:ENU34073.1, ECO:0000313|Proteomes:UP000018426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 1103 {ECO:0000313|EMBL:ENU34073.1,
RC ECO:0000313|Proteomes:UP000018426};
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 parvus NIPH 1103.";
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:ENU34073.1}.
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DR EMBL; APOL01000019; ENU34073.1; -; Genomic_DNA.
DR RefSeq; WP_004677987.1; NZ_KB849225.1.
DR AlphaFoldDB; N8RFB1; -.
DR STRING; 134533.GCA_001485085_01834; -.
DR PATRIC; fig|1217671.3.peg.1041; -.
DR HOGENOM; CLU_038243_0_0_6; -.
DR Proteomes; UP000018426; 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:ENU34073.1};
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 534 AA; 59509 MW; A5A00382AE1CBB8D CRC64;
MSTYLTAIDA IRELKAKFGD TWRDISPEDA ARMQIQNRFK TGLDIAKYTA AIMRRDMAAY
DADSSKYTQS LGCWHGFIAQ QKMIANKKYF GTTERRYIYL SGWMVAALRS EFGPLPDQSM
HEKTSVPALI EEIYTFLRQA DAKELNDLFR ALKKAQEAGD TAKAAEITAQ IDGFQTHVVP
IIADIDAGFG NEEATYLLAK KMIEAGACAL QIENQVSDAK QCGHQAGKVT VPHEDFIAKI
HALRYAFLEM GLDDGIIVAR TDSEGADLTQ KIPVVKEPGD IASQYISYLD TQEIDISEAK
EDEILIKRDG KLHRPKRLAS GLYQFREGTQ IDRVVLDCVT SLQNGADLLW IETATPNVEE
IAHMVNRVRE TVPNAKLVYN NSPSFNWTLN FRQQAYDRWV AEGKDVSAYD RAKLMSAEYD
ETELAADADA KIRTFQADAS REAGVFHHLI TLPTYHTAAL STHELAQGYF GSEGMLAYVA
GVQRKEIRQG IACVKHQAMA GSDIGDDHKE IFSGDNALKA HDDAKNTMNQ FAAH
//
