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Database: UniProt
Entry: A0A1M5SF30_9BACT
LinkDB: A0A1M5SF30_9BACT
Original site: A0A1M5SF30_9BACT 
ID   A0A1M5SF30_9BACT        Unreviewed;       730 AA.
AC   A0A1M5SF30;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05720761_11355 {ECO:0000313|EMBL:SHH36513.1};
OS   Fibrobacter sp. UWCM.
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=1896208 {ECO:0000313|EMBL:SHH36513.1, ECO:0000313|Proteomes:UP000184289};
RN   [1] {ECO:0000313|EMBL:SHH36513.1, ECO:0000313|Proteomes:UP000184289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWCM {ECO:0000313|EMBL:SHH36513.1,
RC   ECO:0000313|Proteomes:UP000184289};
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; FQWR01000013; SHH36513.1; -; Genomic_DNA.
DR   RefSeq; WP_073114977.1; NZ_FQWR01000013.1.
DR   AlphaFoldDB; A0A1M5SF30; -.
DR   Proteomes; UP000184289; 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   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         124..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         340
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         537
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         538
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         542
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   SITE            247
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            410
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   730 AA;  79655 MW;  198733C8DE96579D CRC64;
     MNTKIYYTLT DESPFLATQS LLPIVRGFAK AADIDVKTKN ISLPGRILAA FGKASDDLDF
     LGKLTLEPDA NIIKLPNISA SVPQLKAAIA ELQKNGFDVP DYPDAPANDE EKAIRAKYDK
     VKGSAVNPVL RQGNSDRRAP KAVKNFARNN PHSNGNWNTS VKTHVASMQA DDFYGNEKSI
     TMADADTFKI EFVNEAGEVT ELRAAKPLLK GEIIDATVMR MASLEKFIAN AMAEAKAKGL
     LFSVHLKATM MKVSDPVLFG AFVRVFFKDV FTKYVDLFKE LGIDANNGLG DLYKRLEGNA
     KEAEVKAAID AALAAGPDLA MVDSAKGVTN LHVPSDVIID ASMPAMIRNS GCMWNKEGKL
     QETIACIPDR CYAGIYDETI EFCKQNGAFD PKTMGTVPNV GLMAQGAEEY GSHDKTFVAK
     GKGVIRAVNS KGEVLLQQNV EAGDIFRMCQ AKDAPVRDWV KLAVTRARLS NTPAIFWLDP
     ERAHDREIQK KVEAYLPKHD LNGLDIKIMS PRKAIVETMK RAKAGLDTIG VTGNVMRDYL
     TDLFPILEVG TSAKMLSIVP LMAGGGLYET GAGGSAPKQV QQFLAENYLR WDSLGEYFAL
     VPAFEQVALK DGNKKAKVLA DTLDEANGKI LEFNRTPARK IGELDNRGSH FYLALYWSEA
     LAAQKDDAEL AKKFAPVADA LKAREAEIVA AFAAEQGKPA DIGGYYLPKA DLLKKWMRPV
     AEFNAVIDAL
//
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