ID S5VCX6_STRC3 Unreviewed; 739 AA.
AC S5VCX6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=B446_31275 {ECO:0000313|EMBL:AGS73059.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS73059.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS73059.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
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; CP006259; AGS73059.1; -; Genomic_DNA.
DR RefSeq; WP_020943469.1; NC_021985.1.
DR AlphaFoldDB; S5VCX6; -.
DR STRING; 1214242.B446_31275; -.
DR KEGG; sci:B446_31275; -.
DR PATRIC; fig|1214242.5.peg.6406; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR Proteomes; UP000015423; 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:AGS73059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 82..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 132..139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 546
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 582..583
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 598..600
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 647
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 255
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 418
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 739 AA; 79509 MW; 81C0A6932FD58036 CRC64;
MTDSTIIYTY TDEAPALATH SFLPVIQAYA SQAGVPVTTR DISLAGRIIA VFPEYLNEDQ
RIPDALSELG ELAKTPAANI IKLPNISASI PQLKAAVAEL QGKGYALPDY PDDPKTDEER
EIRARYDKIK GSAVNPVLRE GNSDRRAPAS VKNYAKTHPH RMGAWSSDSK TNVATMGVDD
FRSTEKSVVI SEAGALRIEL KGDDGSTTVL RESVPVLEGE VVDASVMRVA ALREFLTAQV
ARAKEEGVLF SVHLKATMMK VSDPIVFGHV VRAFFPKTFA KYGETFAAAG LTPNDGLGGI
FKGIESLPEG AEIKASFDAE LAEGPALAMV DSDKGITNLH VPSDVIVDAS MPAMIRTSGH
MWGPDGQEAD TLAVLPDSSY AGVYQAVIED CRAHGAYDPS TMGSVPNVGL MAQKAEEYGS
HDKTFEIPVT GTVRLVDQAG NVVIEQTVSA GDIFRACQTK DAPIKDWVKL AVTRARATGD
PAVFWLDETR AHDANLIGKV KQYLAEHDTE GLDIRVLAPV EATKLSVERI RRGENTISVT
GNVLRDYLTD LFPILELGTS AKMLSVVPLM AGGGLFETGA GGSAPKHVQQ LVKENYLRWD
SLGEFFALVP SFEQYATATG NTRAKVLADT LDRATATFLN EDKSPTRRVG GIDNRGSHFY
LSLYWAQELA AQTDDADLAK AFGAFAENLA ANEQTIVDEL IAVQGKPADI GGYYRPEKAK
ADAVMRPSAT WNEALASLS
//
