ID R4YWI6_9ACTN Unreviewed; 747 AA.
AC R4YWI6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CCM62300.1};
GN ORFNames=BN381_100187 {ECO:0000313|EMBL:CCM62300.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM62300.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM62300.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM62300.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(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}.
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:CCM62300.1}.
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DR EMBL; CANL01000002; CCM62300.1; -; Genomic_DNA.
DR RefSeq; WP_012223544.1; NZ_HG422565.1.
DR AlphaFoldDB; R4YWI6; -.
DR STRING; 1229780.BN381_100187; -.
DR GeneID; 78312812; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_11; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000018291; 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 ECO:0000313|EMBL:CCM62300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018291};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 88..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 138..145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 554
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 558
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 590..591
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 595
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 606..608
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 655
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 261
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 426
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 747 AA; 79198 MW; 7DF47528D028B4BC CRC64;
MSDATKPTAS TIIYTLTDEA PALATRSLLP VIAAFAGASG VNVETRDISL AGRILAAFSD
RLPAEQRRDD HLAELGELVT MPEANIIKLP NISASLPQLK EAVAELQADG YDLPDYPDEP
ATDAEVEVLA RYASVMGSAV NPVLREGNSD RRAPAAVKAY ARNHPHSMGA WSPDSKTRVA
TMTDGDFRST ERSVTVADDD SLSIRFTPTD GEARELRAPV SVSAGTIVDG SLMSAAALDE
FLTAAIARAK AEGVLWSIHL KATMMKVSDP IMFGHAVRAF FPGLFAEYGD VLAEAGFNPN
NGLASLDAAI NNLPVDARTS VESALAAGYA AGPELAMVNS DKGITNLHVP SDVIIDASMP
AMIRTSGQMW GPDGESADTL AVIPDHSYAG VYAEAIDFCR ANGALDPTTM GSVPNVGLMA
QKAEEYGSHD KTFEIESDGV VEVLDGAGDV LLTHQVSTGD IWRMCLAADA PVRDWVSLAV
RRARATGAPA VFWLDETRAH DAALIAKVNA YLGDEDTEGL DIRTMTPEAA THFSLERIVD
GLDTISVTGN VLRDYLTDLF PILEVGTSAK MLSIVPLMAG GGLFETGAGG SAPKHVQQFV
AENHLRWDSL GEFLALGASL EHLADSTDNA RARLLSTTLD DATARVLEED RSPSRKVNEL
DNRGSHFYLA LYWAEALAAQ AEDAGLAAVF ASLATQLAEA ETTIVDELNS VQGNPVDLGG
YYWPKPQAAT DAMRPSATLN AILDGFS
//
