ID C3PLB9_CORA7 Unreviewed; 727 AA.
AC C3PLB9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 Name=icd {ECO:0000313|EMBL:ACP32123.1};
GN OrderedLocusNames=cauri_0526 {ECO:0000313|EMBL:ACP32123.1};
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP32123.1, ECO:0000313|Proteomes:UP000002077};
RN [1] {ECO:0000313|EMBL:ACP32123.1, ECO:0000313|Proteomes:UP000002077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC {ECO:0000313|Proteomes:UP000002077};
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP32123.1; -; Genomic_DNA.
DR RefSeq; WP_010189398.1; NZ_ACLH01000061.1.
DR AlphaFoldDB; C3PLB9; -.
DR STRING; 548476.cauri_0526; -.
DR GeneID; 31923145; -.
DR KEGG; car:cauri_0526; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000002077; Chromosome.
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 ECO:0000313|EMBL:ACP32123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 79..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 120..127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 533
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 537
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 569..570
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 574
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 585..587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 634
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 242
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 405
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 727 AA; 78702 MW; EDB2A43E5306F45E CRC64;
MAKIIWTRTD EAPLLATYSF KPVVEAFAST AGIEVETRDI SLAGRILAQF PERLGDKKVS
DALAELGELA KTPEANIIKL PNISASLVQL KKAIAELQAA GYDLPEYEEA QEKYDAVKGS
AVNPVLREGN SDRRAPIAVK NFAKKNPHKM GAWSADSKTN VATMDANDFR HNEKSVIMPE
EDTLSIVLKT AEGEQTLLEK LPVLKGEVID GTFMSAKALD EFLKAQVARA KEEGVLFSAH
LKATMMKVSD PIIFGHVVRA FFADVFEKYG EELEAAGLNG ENGLGAIYEG LDKLENGAEI
KAAFDAALAA GPDLAMVNSH KGITNLHVPS DVIIDASMPA MIRTSGHMWN KNDEEQDTLA
VIPDSSYAGV YQAVIEDCKA NGAYDPTTMG TVPNVGLMAQ KAEEYGSHNK TFKIPAAGTV
EVRNSKGEAL ISHDVEAGDI WRACQTKDAP IQDWVKLAVN RARLSGMKAI FWLDPERGHD
ANLIELVKKY LADHDTEGLD ISIEDPVTAT KISVERIRKG EDTISVTGNV LRDYNTDLFP
ILELGTSAKM LSVVPLMAGG GLFETGAGGS APKHVQQVQE ENHLRWDSLG EFLALAESFR
HEHNTNGNAK AGVLAAALDK ATETLLDEGK SPSRKVGEND NRGSHFFLTL NWAKELAAQS
DDAELAEAFK PVAEALEAKA GEIEQALLDV QGSPVDLGGY YAPNEEKLNE TMRPVAAFNE
IIDGLKK
//
