ID A0A090QQ99_9FLAO Unreviewed; 750 AA.
AC A0A090QQ99;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=JCM19294_202 {ECO:0000313|EMBL:GAK97666.1};
OS Nonlabens tegetincola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=323273 {ECO:0000313|EMBL:GAK97666.1, ECO:0000313|Proteomes:UP000029221};
RN [1] {ECO:0000313|EMBL:GAK97666.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19294 {ECO:0000313|EMBL:GAK97666.1};
RA Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W.,
RA Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L.,
RA Niwa A., Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains NR17,
RT NR24, NR27, NR32, NR33, and Ara13.";
RL Genome Announc. 2:e01165-14(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK97666.1}.
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; BBML01000006; GAK97666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090QQ99; -.
DR STRING; 319236.BST91_06470; -.
DR eggNOG; COG2838; Bacteria.
DR Proteomes; UP000029221; 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 ECO:0000313|EMBL:GAK97666.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029221};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT REGION 150..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 144..151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 559
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 560
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 564
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 596..597
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 601
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 612..614
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 661
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 267
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 432
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 750 AA; 82518 MW; B506FE0BD5C9194C CRC64;
MFITLKNRII TMADLPKIIY TKTDEAPALA TASFLPIIKK FIAPAGIDID TADISLAGRI
IATFPENLTE DQKQEDALAQ LGELVKQPDA NVIKLPNISA SIPQLTAAIA ELQALGYNLP
DYPEDPQTEE EKEIQKRYNK IKGSAVNPVL REGNSDRRAP KPVKQYAKNN PHSMGAWSSD
SKSHVATMSA GDFAHNEKSH TFEESTSVSI QLVKNDGETE VLKSGLNLQK GEILDATYMS
KNALLSFLKE QIEDAKSQGV LFSLHMKATM MKVSDPIIFG HAVRTFFAPV FEKFGTELEE
AGVDVNNGFG DLLSKLDQLP GDVQTAIEKE IEKVYEQRPD IAMVNSDKGI TNLHVPSDVI
IDASMPAMIR TSGQMWNKAG ETQDTKAVIP DSSYAGIYQE TIQFCKEHGA FDPTTMGTVP
NVGLMAQKAE EYGSHDKTFE IQANGKVQVV SENGTVIIEH DVEEGDIWRA CQTKDAPIQD
WVKLAVSRAR ATNDPAIFWL DENRAHDAEL IKKVNTYLKD HDTEGLDISI ASPVEATKRT
LARMKDGLNT ISVTGNVLRD YNTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK
HVQQFEKENH LRWDSLGEFL ALAVSLEHLA EKYDNKKAQI LADSLDRATE KFLTNKKSPS
RKVNELDNRG SHFYLALYWA QELASQNQDE ELSAQFSSLA KQLSDNEEVI NKELIDAQGV
AMDIGGYYRP DAAKESAAMR PSATLNSIIG
//
