ID A0A0A8E5U6_9GAMM Unreviewed; 738 AA.
AC A0A0A8E5U6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=SD28_06810 {ECO:0000313|EMBL:AJC49349.1};
OS Allofrancisella guangzhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Allofrancisella.
OX NCBI_TaxID=594679 {ECO:0000313|EMBL:AJC49349.1, ECO:0000313|Proteomes:UP000031104};
RN [1] {ECO:0000313|EMBL:AJC49349.1, ECO:0000313|Proteomes:UP000031104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08HL01032 {ECO:0000313|EMBL:AJC49349.1,
RC ECO:0000313|Proteomes:UP000031104};
RA Svensson D., Ohrman C., Backman S., Karlsson E., Nilsson E., Bystrom M.,
RA Larkeryd A., Stenberg P., Scholtz H.C., Forsman M., Sjodin A.;
RT "Complete genome sequence of Francisella guanzhouensis strain 08HL01032
RT isolated from air-conditioning system in China.";
RL Submitted (DEC-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010427; AJC49349.1; -; Genomic_DNA.
DR RefSeq; WP_039125329.1; NZ_JACVKK010000002.1.
DR AlphaFoldDB; A0A0A8E5U6; -.
DR STRING; 594679.SD28_06810; -.
DR KEGG; fgu:SD28_06810; -.
DR HOGENOM; CLU_025308_1_0_6; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000031104; Chromosome.
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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
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 ECO:0000313|EMBL:AJC49349.1};
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 738 AA; 81931 MW; 332F2345E704FDEF CRC64;
MHKIFYTMTD EAPALATGSF LPIAQSFTKL ADIALETKDI SLASRILANF NDYLTDQQKC
SDDLAILGEL AKTPDANIIK LPNISASVPQ LTAAIKELQT KGYDIPDYPF EPKDEKEQEI
KSRYSKVLGS AVNPVLREGN SDRRVAAAVK AYAQKHPHSM GEWTKDSKSH VASMSDNDFY
ANEKSYIVPK AMTVKIVHID NKGKETVLKA GLKLEEKEII DATKISAKAL REFYKQEIQN
AKKEGTLLSL HLKATMMKVS DPILFGHAVE IFFEDVFKKY AKEFKELGVN PRNGWGDAVE
KIKQLPQELQ DKINADIEKV FTKQPDIAMV NSDKGITNLN VPSDVIIDAS MPAAIRSSGK
MWNKNGQLQD IKAMIPDRCY AGVYAATIGF CRENGAFDVA TMGDVSNVGL MAKKAEEYGS
HDKTFEIQAD GKVLVIDAED NVIFEHGVEE GDIWRACQTK DIAVKDWVKL AVNRAKVTQN
PAIFWLDAKR AHDRNLIAKV HEYLTLHDTT GLNIEILSPV EATKYSLKRM KEGKDTISVT
GNVLRDYLTD LFPILELGTS AKMLSIVPLL AGGGLFETGA GGSAPKHVEQ LINENHLRWD
SLGEFLALGA SLEDLAIKTR DPKIKVLAEG LGQANKDFLD NDKSPRRKVG ELDTRGSHFY
LAFYWAKALA EQNGEQELKA KFEPIYQELK ANEEKIVREL ASVQGKKVDI GGYYLPESSK
LGSVMRPSKT FNNILTKV
//