ID N6ZMQ1_9RHOO Unreviewed; 746 AA.
AC N6ZMQ1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=C667_18157 {ECO:0000313|EMBL:ENO95608.1};
OS Thauera phenylacetica B4P.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1234382 {ECO:0000313|EMBL:ENO95608.1, ECO:0000313|Proteomes:UP000013047};
RN [1] {ECO:0000313|EMBL:ENO95608.1, ECO:0000313|Proteomes:UP000013047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4P {ECO:0000313|EMBL:ENO95608.1,
RC ECO:0000313|Proteomes:UP000013047};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) 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 -!- 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:ENO95608.1}.
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DR EMBL; AMXF01000194; ENO95608.1; -; Genomic_DNA.
DR RefSeq; WP_004373172.1; NZ_AMXF01000194.1.
DR AlphaFoldDB; N6ZMQ1; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000013047; 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};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW ECO:0000313|EMBL:ENO95608.1};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
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 550
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 555
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
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 746 AA; 82886 MW; 3A355A2D903DA6E7 CRC64;
MSAGKSKIIY TLTDEAPLLA TCAFLPIIRT FTGPAGVEVE KADISVSARV LAEFPEYLSE
DQRVPDTLAE LGRLTLEPDT NIIKLPNISA SVAQLKACVK ELQEKGYKIP DYPEDPKTDE
EKALRARFGK CLGSAVNPVL REGNSDRRAP AAVKNFAKKH PHSMGEWKQW SQTHVSHMHH
GDFYHGEKSM TLDRARSVKM ELITKSGKAV VLKPRTDLLD GEIIDSMFMS KKALCEFYEK
ELDDCREAGI LFSLHVKATM MKVSHPIVFG HCVKIYYKDA FAKHGKLFDE LGINVNNGMV
DLYEKIKTLP ESKHDEIIRD LHACNEHRPE LAMVDSAKGI TNFHSPNDII VDASMPAMMR
QGGKMWGSDG KQYDSKCVMP ESTFARIYQE MINFCKWHGN FDPRTMGTVP NVGLMAQKAE
EYGSHDKTFE ITEDGVANIT DLATGEVLLS QNVEAGDIWR MCQVKDAPIR DWVKLAVTRA
RNSGMPAIFW LDPYRPHENE LIKKVKVYLK DHDTSGLDIQ IMSQVRAMRF TLERVARGLD
TISVTGNILR DYLTDLFPIM ELGTSAKMLS IVPLMNGGGM YETGAGGSAP KHVQQLVQEN
HLRWDSLGEF LALAVSLEDL GIKTGNVRAK LLAKTLDEAT GRLLDENKSP SPKTGQLDNR
GSQFYLALFW AERLAAQTED AELAGKFAPL AKALRENEGK IVEELAVVQG KPADIGGYYK
ADAEKTKAIM RPSATLNAIL KGARAA
//
