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Database: UniProt
Entry: A0A255GCN8_9ACTN
LinkDB: A0A255GCN8_9ACTN
Original site: A0A255GCN8_9ACTN 
ID   A0A255GCN8_9ACTN        Unreviewed;       737 AA.
AC   A0A255GCN8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=CGZ94_11865 {ECO:0000313|EMBL:OYO13648.1};
OS   Enemella evansiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Enemella.
OX   NCBI_TaxID=2016499 {ECO:0000313|EMBL:OYO13648.1, ECO:0000313|Proteomes:UP000215896};
RN   [1] {ECO:0000313|EMBL:OYO13648.1, ECO:0000313|Proteomes:UP000215896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 030167 {ECO:0000313|EMBL:OYO13648.1,
RC   ECO:0000313|Proteomes:UP000215896};
RA   Bernier A.-M., Bernard K., Domingo M.-C.;
RT   "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL   Submitted (JUL-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}.
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:OYO13648.1}.
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DR   EMBL; NMVO01000013; OYO13648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255GCN8; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000215896; 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   Reference proteome {ECO:0000313|Proteomes:UP000215896};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         80..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         130..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         346
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         543
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         544
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         548
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         580..581
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         585
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         596..598
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         645
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            253
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            416
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   737 AA;  80034 MW;  FA1EA2CBC2AD628F CRC64;
     MPKIIYTLTD EAPMLATFSF KPIVDAFAAA AGVEVEARDI SLAGRILAAF ADRLPSDQRV
     ADALAELGEL AKTPDANIIK LPNISASVPQ LKAAVAELKA QGFDLPDYPE SPQSEADKEI
     RARYDAVKGS AVNPVLREGN SDRRAPAAVK NYARKHPHSM GAWTPESKTE VATMSDHDFR
     HNEDSVIIPA ADTLQIRLEA NDGSTTVLKE SIPVLEGEVI DATFLSAGEL DEFLAEQIRR
     AKEQDLLFSV HLKATMMKVS DPIIFGHVIK IFFDEVFAKY GDDLAAAGLS PNDGLAAIFA
     GLEKLPNSAE IRAAFDQAIA DGPRLAMVNS DKGITNLHVP SDVIVDASMP AMIRTSGQMW
     GPDGNQADTL AVIPDSSYAG IYQAVIDDCR KHGAYDPTTM GSVPNVGLMA QKAEEYGSHD
     KTFEIPAAGR VQIVNSTGEV LTEHQVEAGD IWRACQTKDA PIRDWVKLAV DRARASETPA
     VFWLDETRSH DQNLITLVKK YLAELDTDGL DIQIMSPIDA ARFSVERIRA GKDTISVTGN
     VLRDYNTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQLI AEDYLRWDSL
     GEFLALAESL RHLAGTYDNA GARVLGDALD KATETLLNEN KSPARKLGQI DNRGSHFWLA
     RYWAEELAKQ TEDPELAKKF QPVAEQLVAQ TDAIDAELIG VQGKPADIGG YYRPDEDKTI
     AVMRPSQTLN EIIDQLR
//
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