ID A0A191V6E4_9ACTN Unreviewed; 739 AA.
AC A0A191V6E4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=GCM10010220_58560 {ECO:0000313|EMBL:GGR98233.1},
GN Spa2297_28605 {ECO:0000313|EMBL:ANJ10591.1};
OS Streptomyces parvulus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ10591.1, ECO:0000313|Proteomes:UP000078468};
RN [1] {ECO:0000313|EMBL:ANJ10591.1, ECO:0000313|Proteomes:UP000078468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2297 {ECO:0000313|EMBL:ANJ10591.1,
RC ECO:0000313|Proteomes:UP000078468};
RA Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA Takahashi H., Shirai M.;
RT "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT Integrated Site-Specifically with Actinophage R4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGR98233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR98233.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGR98233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR98233.1};
RA Sun Q., Ohkuma M.;
RL Submitted (DEC-2022) 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; CP015866; ANJ10591.1; -; Genomic_DNA.
DR EMBL; BMRX01000016; GGR98233.1; -; Genomic_DNA.
DR RefSeq; WP_064730914.1; NZ_JAMOLM010000072.1.
DR AlphaFoldDB; A0A191V6E4; -.
DR KEGG; spav:Spa2297_28605; -.
DR Proteomes; UP000078468; Chromosome.
DR Proteomes; UP000645274; 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 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; 79519 MW; 4419405881E79CBC CRC64;
MTDSTIIYTH TDEAPALATY SFLPVIRAYA SQAGVAVETR DISLAGRIIS LFPEYLTEDQ
RIPDALAELG ELAKTPAANI IKLPNISASI PQLKAAIAEL QGQGYALPAY PDDPKTDEER
DVRARYDKVK GSAVNPVLRE GNSDRRAPAS VKNYAKNHPH RMGAWTGESK TNVATMGEND
FRSTEKSVVV AEDGALRIEL VGDDGTTTVL RESVPVKKDE VLDASVLRVA ALREFLTAQV
ARAKAEGILY SVHLKATMMK VSDPIIFGHV VRAFFPKTFA QFGDKLAAAG LTPNDGLGGI
YKGLESLPEG AEIKASFDAE LAEGPELAMV DSDKGITNLH VPSDVIIDAS MPAMIRTSGH
MWGADGQEHD ALAVIPDSSY AGVYQAVIDD CRAHGAYDPS TMGSVPNVGL MAQKAEEYGS
HDKTFEIPTT GTVRLVGADG EPVLEQTVSA GDIFRACQTK DAPIRDWVKL AVTRARATGD
PAVFWLDEGR AHDANLIAKV KQYLPEHDTE GLDIKILSPV EATKLSVERI RRGENTISVT
GNVLRDYLTD LFPILELGTS AKMLSVVPLM AGGGLFETGA GGSAPKHVQQ LVKEDYLRWD
SLGEFFALVP SLEQYAETTG NTKARVLADA LDRATATFLN EDKSPTRRVG GIDNRGSHFY
LSLYWAQELA KQTDDADLAK AFAPLAETLT AAEQKIVDEL NAVQGKPAEI GGYYQPDPAK
AAAVMRPSAT WNEALASLA
//
