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Database: UniProt
Entry: A0A0S8CSC6_9BACT
LinkDB: A0A0S8CSC6_9BACT
Original site: A0A0S8CSC6_9BACT 
ID   A0A0S8CSC6_9BACT        Unreviewed;       744 AA.
AC   A0A0S8CSC6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 22.
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=AMK69_11250 {ECO:0000313|EMBL:KPK26933.1};
OS   Nitrospira bacterium SG8_3.
OC   Bacteria; Nitrospirota; Nitrospiria.
OX   NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK26933.1, ECO:0000313|Proteomes:UP000051394};
RN   [1] {ECO:0000313|EMBL:KPK26933.1, ECO:0000313|Proteomes:UP000051394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_3 {ECO:0000313|EMBL:KPK26933.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK26933.1}.
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DR   EMBL; LJNR01000173; KPK26933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8CSC6; -.
DR   PATRIC; fig|1704023.3.peg.342; -.
DR   Proteomes; UP000051394; 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; 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:KPK26933.1};
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         353
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   BINDING         587..588
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         592
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         603..605
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         652
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            258
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            423
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   744 AA;  81075 MW;  F1AACDE396713EF4 CRC64;
     MSAQPDIIYT KVDEAPELAS GSFLPIIQSF AKAAGVTVGT KDISLAGRIL AQFSDKLKPE
     QRQPDDLALL GELVEKPEAN VIKLPNISAS LPQIKGAIAE LQSQGYAVPD YPEDPKNDEE
     KEIKAKYDKV KGSAVNPVLR QGNSDRRASA SVKQYAKKNP HKMGKWTKDS RTHVAHMTSG
     DFFGNEKSAT ITDQTAGQGR IEFVAGDGSV KVLKDKLTLK AGDVLDASVM SCRALRQFLK
     EQVADAKQSG ILWSLHLKAT MMKVSDPIMF GHAVTVYFED VFKKHEKVFN ELGVNPSNGL
     GDVYAKIGKL PAAQQEEIKA DIQAALKNGP ALAMVDSDKG ITNLHVPSDI IIDASMAAAL
     RTSGKMWGPD GKEHDMKAIV PDRSYAGIYQ AVVEFCRENG EFNPSTMGSV PNVGLMAQKA
     EEYGSHDKTF EATGKGVIRV IDGAGKVLLQ HDVEKGDIWR SCYTTDISIK DWVKLAVNRA
     RASSTPVVFW LNKNRAHDAQ LIEKVNRYLK DHDTKGLDIQ IMAPNDAMKH SLERAKKGLD
     TISATGNVLR DYLTDLFPIL ELGTSAKMLS IVPLINGGGL FETGAGGSAP KHVQQFVKEG
     HLRWDSLGEF LALSESFAHL GQTKANKKAK VLAETLDRAT GKLMENRKAP GRELGQLDNI
     GSHVYEALYW AQELAAQNDD LDLKKQFAPI SKELESKIDV ILEEIKAAKG RAQDIGGYYH
     PDAAKVKAAM RPSATLNKIL ESVA
//
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