ID A0A0P1FKT9_THAGE Unreviewed; 740 AA.
AC A0A0P1FKT9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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_2 {ECO:0000313|EMBL:CUH68739.1};
GN ORFNames=TG4357_03768 {ECO:0000313|EMBL:CUH68739.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH68739.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH68739.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH68739.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYSA01000028; CUH68739.1; -; Genomic_DNA.
DR RefSeq; WP_058264420.1; NZ_FOFW01000006.1.
DR AlphaFoldDB; A0A0P1FKT9; -.
DR STRING; 53501.SAMN04488043_106229; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000051587; 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:CUH68739.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 85..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 135..142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 554
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 586..587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 591
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 602..604
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 651
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 260
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 423
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 740 AA; 78700 MW; B93C7577A076077E CRC64;
MAENSNPDIL YTIVDEAPEL ASASFLPIIR TFASAAGVSV GTKDISLAGR LLATFPENLT
DEQRHSDDLA ELGELVKTPG ANVIKLPNIS ASVPQLVAAV TELQSQGYDI PNYPEDPKTD
AEKAIRARFD AIKGSAVNPV LREGNSDRRA AKAVKNYAQK NPHRMGAWAS DSKTHVSSML
GNDFYANEVA TTLSADQAGS AKIEVVGKDG SVTVLKDGWT LIEGEVVDAT FMSAKALGAF
LTDEIEASKK DGTLFSIHLK ATMMKVSDPI IFGHAVKAWL APVFDKYGDQ LAAAGVNPNS
GMGDVLARIA DMDNAAAILA DIDALNAERP AMYMVNSDKG ITNLHVPSDV IIDASMPALI
RAGGKGWGPD GKEGDTNCVI PDNCYATVYD EAVEFFKTNG ALNPATAGTV QNVGLMAQKA
EEYGSHPTTF EAPADGAIRI VLANGEVLHS LDVEAGDIWR ACSAKKAPIE NWIQLAIDRQ
RLTGFQAIFW LDENRGHDAE IIKYVKPALD AAGVADKFVI MAPREATRAS LETITAGKDS
IAITGNVLRD YLTDLFPILE LGTSAKMLSI VKLMNGGGMF ETGAGGSAPK HVQQLLEENH
LRWDSMGEFC ALSESLNFLA DSKGNAKAGV LATAAEAATQ GILDDNRSPS RKVGEPDNRD
SHYWFARYWA EALAAQTDDA ELAAHFAPIA KQLAEKESAI LAELAAAQGG AGDIGGYYHP
SMELKAKVMR PSATLNAIIG
//
