ID A0A1M5H4C6_9FLAO Unreviewed; 739 AA.
AC A0A1M5H4C6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05443633_11075 {ECO:0000313|EMBL:SHG10743.1};
OS Chryseobacterium arachidis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1416778 {ECO:0000313|EMBL:SHG10743.1, ECO:0000313|Proteomes:UP000184518};
RN [1] {ECO:0000313|EMBL:SHG10743.1, ECO:0000313|Proteomes:UP000184518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27619 {ECO:0000313|EMBL:SHG10743.1,
RC ECO:0000313|Proteomes:UP000184518};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUT01000010; SHG10743.1; -; Genomic_DNA.
DR RefSeq; WP_072960562.1; NZ_FQUT01000010.1.
DR AlphaFoldDB; A0A1M5H4C6; -.
DR STRING; 1416778.SAMN05443633_11075; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000184518; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 2.
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 Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 83..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 133..140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 546
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 547
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 583..584
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 588
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 599..601
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 648
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 256
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 419
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 739 AA; 80764 MW; EB78D960331E769A CRC64;
MSDKSKIYYT LTDEAPMLAT HSFLPIVKAF TKSANIEIAV PDISLAGRIL ANFPEFLNDD
QKIGDALAEL GQLATQPDAN IIKLPNISAS APQLDAAIAE LQAKGFAVPN YPSEPKNEEE
KAIKAKYAKV LGSAVNPVLR EGNSDRRAPK AVKNYAKANP HRMGNWASDS KTDVAHMIGG
DFYGTETSTT LENATKYKIV FKANDGTETQ LKDYASLQAG EVIDSSVMNL NALKAFVQEA
IEEAKNRNVL LSAHLKATMM KISDPIIFGA IVETFFKEVF TKYAETFKSL DINPNNGLAD
LFDKIKGNAQ EAEIKADIEA ALANGPRVAM VNSDKGITNF HVPSDIIVDA SMAALVRGGG
KMWNKDGNEE DTVAIIPDRS YAGFYQAVID DMKAHGKLDP TTMGSVPNVG LMAQKAEEYG
SHDKTFQVSA EGTVEVQDEN GNVLLSQKVE KGDIFRMCQT KDAPIQDWVK LAVNRARLSD
TPAIFWLDKG RAHDREMIKK VEKYLADHDT NGLDIKILDV KDAMTETLRR AREGKDTISV
SGNVLRDYLT DLFPILELGT SAKMLSIVPL MNGGGLFETG AGGSAPKHVE QFIEEGYLRW
DSLGEFLALQ ASLEHLAQTQ NNTKSQVLAD ALDEANAKFL ATDKSPARKV GEIDNRGSHF
YLAMYWAEAL ANQTADAELA QQFAPIAEAM KENEEVINAE LIGAQGKPQD IEGYYKTDTY
KTYAAMRPST VLNEIIDGI
//
