ID A1E5X1_MYXXA Unreviewed; 181 AA.
AC A1E5X1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE Flags: Fragment;
GN Name=icd {ECO:0000313|EMBL:ABL61896.1};
OS Myxococcus xanthus.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34 {ECO:0000313|EMBL:ABL61896.1};
RN [1] {ECO:0000313|EMBL:ABL61896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B129 {ECO:0000313|EMBL:ABL61919.1}, B130
RC {ECO:0000313|EMBL:ABL61920.1}, B70 {ECO:0000313|EMBL:ABL61896.1}, B71
RC {ECO:0000313|EMBL:ABL61897.1}, B72 {ECO:0000313|EMBL:ABL61898.1}, B74
RC {ECO:0000313|EMBL:ABL61899.1}, B75 {ECO:0000313|EMBL:ABL61900.1}, B76
RC {ECO:0000313|EMBL:ABL61901.1}, B77 {ECO:0000313|EMBL:ABL61902.1}, B78
RC {ECO:0000313|EMBL:ABL61903.1}, B80 {ECO:0000313|EMBL:ABL61905.1}, B83
RC {ECO:0000313|EMBL:ABL61907.1}, B84 {ECO:0000313|EMBL:ABL61908.1}, B90
RC {ECO:0000313|EMBL:ABL61912.1}, B92 {ECO:0000313|EMBL:ABL61914.1}, B93
RC {ECO:0000313|EMBL:ABL61915.1}, and B99 {ECO:0000313|EMBL:ABL61917.1};
RX PubMed=18328701; DOI=10.1016/j.cub.2008.02.050;
RA Vos M., Velicer G.J.;
RT "Isolation by distance in the spore-forming soil bacterium Myxococcus
RT xanthus.";
RL Curr. Biol. 18:386-391(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; EF111265; ABL61896.1; -; Genomic_DNA.
DR EMBL; EF111266; ABL61897.1; -; Genomic_DNA.
DR EMBL; EF111267; ABL61898.1; -; Genomic_DNA.
DR EMBL; EF111268; ABL61899.1; -; Genomic_DNA.
DR EMBL; EF111269; ABL61900.1; -; Genomic_DNA.
DR EMBL; EF111270; ABL61901.1; -; Genomic_DNA.
DR EMBL; EF111271; ABL61902.1; -; Genomic_DNA.
DR EMBL; EF111272; ABL61903.1; -; Genomic_DNA.
DR EMBL; EF111274; ABL61905.1; -; Genomic_DNA.
DR EMBL; EF111276; ABL61907.1; -; Genomic_DNA.
DR EMBL; EF111277; ABL61908.1; -; Genomic_DNA.
DR EMBL; EF111281; ABL61912.1; -; Genomic_DNA.
DR EMBL; EF111283; ABL61914.1; -; Genomic_DNA.
DR EMBL; EF111284; ABL61915.1; -; Genomic_DNA.
DR EMBL; EF111286; ABL61917.1; -; Genomic_DNA.
DR EMBL; EF111288; ABL61919.1; -; Genomic_DNA.
DR EMBL; EF111289; ABL61920.1; -; Genomic_DNA.
DR AlphaFoldDB; A1E5X1; -.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 1..181
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT SITE 97
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 169
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 37
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL61896.1"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:ABL61896.1"
SQ SEQUENCE 181 AA; 20233 MW; 47A23F27FA3923F8 CRC64;
KIAWYEVLAG EKSFKAVNNW LPDETVEAFR TYLVGIKGPL TTPVGGGIRS LNVALRQMLD
LYVCLRPVRY FKGVPSPVKT PDKVDMTIFR ENTEDIYAGI EFEAGTAAAE KFLGILKQEF
PKEFGKIRFP SDVGLGVKPV SHEGSDRLIR AAIQYAVDHK RKSVTLVHKG NIMKFTEGAF
R
//
