ID A0A1K2IQA3_9FLAO Unreviewed; 736 AA.
AC A0A1K2IQA3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN ORFNames=SAMN05428642_104279 {ECO:0000313|EMBL:SFZ94612.1};
OS Flaviramulus basaltis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flaviramulus.
OX NCBI_TaxID=369401 {ECO:0000313|EMBL:SFZ94612.1, ECO:0000313|Proteomes:UP000182544};
RN [1] {ECO:0000313|EMBL:SFZ94612.1, ECO:0000313|Proteomes:UP000182544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18180 {ECO:0000313|EMBL:SFZ94612.1,
RC ECO:0000313|Proteomes:UP000182544};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR009407-3};
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC {ECO:0000256|PIRNR:PIRNR009407}.
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DR EMBL; FPKV01000004; SFZ94612.1; -; Genomic_DNA.
DR RefSeq; WP_072403449.1; NZ_FPKV01000004.1.
DR AlphaFoldDB; A0A1K2IQA3; -.
DR STRING; 369401.SAMN05428642_104279; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000182544; Unassembled WGS sequence.
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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR NCBIfam; TIGR00178; monomer_idh; 1.
DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW Reference proteome {ECO:0000313|Proteomes:UP000182544};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 80..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 130..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 546
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 582..583
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 598..600
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 647
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 253
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 418
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 736 AA; 80756 MW; AAA4ECE71B44901B CRC64;
MSKIIYTKTD EAPALATRSF LPIVKAYVKS SGINIETKDI SLAARILAVF PDFLNEDQKV
SDDLAILGEL AKKPEANIIK LPNISASIPQ LKAAIKELQS QGFKIPNYPD EAENNTEKDI
KSRYDKIKGS AVNPVLREGN SDRRAPKAVK NYAKKNPHSM GAWSSDSKTH VATMDAGDFA
HNEKSVTIKD ATSIKIEHTD SHGKITILKD SFPLLKGEII DATVMSKKAL ISFFETQVAD
AKAKGVLFSL HMKGTMMKVS DPIIFGHAVK VFLKDVFAKY NNTFNKIGVD VNNGFGNLVE
KLKELPEAEQ KEIQAAIDAA FDKGPSIAMV NSDKGITNLH VPSDVIIDAS MPAMIRTSGQ
MWNADGKLQD TKAVIPDSSY AGIYSATIDF CKKHGAFDPT TMGTVPNVGL MAQKAEEYGS
HDKTFEIPSN GTVKVIDASG NVLLQHNVET GDIWRMCQTK DAPIQDWVKL AVTRARASET
PAVFWLDENR AHDAELIKKI NTYLKDHDTS GLDLRILSPI DATIFTCERL IKGEDTISVS
GNVLRDYLTD LFPILEVGTS AKMLSIVPLM NGGGLFETGA GGSAPKHVQQ LLEENHLRWD
SLGEFLALAV SLEHFSEVNN NSKAKILGET LDDATEKLLE NKKGPSRKAG ELDNRGSHFY
LAMYWAQELA SQNKDEALKK EFTSIAKKLA DNESTIIKEL NDIQGNPVSI GGYYEPNEAL
INQVMRPSKT FNSILE
//
