ID A0A1N7NJD6_9BACT Unreviewed; 742 AA.
AC A0A1N7NJD6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05421761_11072 {ECO:0000313|EMBL:SIS98381.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS98381.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIS98381.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS98381.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTOP01000010; SIS98381.1; -; Genomic_DNA.
DR RefSeq; WP_076501793.1; NZ_FTOP01000010.1.
DR AlphaFoldDB; A0A1N7NJD6; -.
DR STRING; 529505.SAMN05421761_11072; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000186026; 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 Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 84..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 549
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 553
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 585..586
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 590
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 601..603
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 650
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 257
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 422
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 742 AA; 81116 MW; 63871F4E53DA1991 CRC64;
MTTKTAKILY TLTDEAPALA TYSLLPIVKA FTDSAGVAVE TRDISLSGRI ISQFPDFLKP
EQQINDALAE LGEIAKTPEA NIVKLPNISA SIPQLKAAIK ELQAQGYALP NYPDDPKTDQ
EKDIKARYDR VKGSAVNPVL REGNSDRRAP LAVKNYAKKN PHSMGAWSAD SKSHVASMSQ
GDFYGSEKSV TVAKATSVDI EFVSATGEVK PLKKGLALKS GEVIDASVLS ISELVAFLQS
QKEAAKKEGV LFSLHMKATM MKVSDPIIFG HAVKVFFAPV FEKYAQLIKD LGVDVNNGFG
DLISKISTLP ADQKAAIEAD IEACLGEGPD LAMVNSDKGI TNLHVPSDVI IDASMPAMIR
TSGQMWNKAG KQQDTKAIIP DRSYAGIYQE TIDFCKQHGA FDPATMGSVP NVGLMAQKAE
EYGSHDKTFE LEADGVVRVV SGDQVLISHE VKQGDIWRMC QTKDAPIQDW VKLAVNRARA
TRDPAIFWLD ENRAHDRELI KKVNTYLQDH DTKGLEIHIM SPVEATRFSL ERIKAGKDTI
SVTGNVLRDY LTDLFPILEL GTSAKMLSFV PLMNGGGLFE TGAGGSAPKH VEQLVEENHL
RWDSLGEFLA LAVSLEHLSA TFSNEKAKVL AETLDQATGK FLEEDKSPSR KVKELDNRGS
HFYLAMYWAE ALAAQDKDAE LKSKFGPIAK EMKDKEAQIL TELNEAQGVK VDIGGYYKPN
EEKTSSVMRP SRTLNAILSK IA
//
