ID H9UIG1_SPIAZ Unreviewed; 745 AA.
AC H9UIG1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 OrderedLocusNames=Spiaf_1226 {ECO:0000313|EMBL:AFG37304.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG37304.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(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; CP003282; AFG37304.1; -; Genomic_DNA.
DR AlphaFoldDB; H9UIG1; -.
DR STRING; 889378.Spiaf_1226; -.
DR KEGG; sfc:Spiaf_1226; -.
DR PATRIC; fig|889378.3.peg.1225; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_12; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000007383; 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 Reference proteome {ECO:0000313|Proteomes:UP000007383};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 81..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 131..138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 546
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 547
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 583..584
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 588
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 599..601
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 648
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 254
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 419
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 745 AA; 81279 MW; 5EDE71D169A502AB CRC64;
MKQVIVYTQT DEAPALATHS FLPVIKTFAD AVGVAVETRD ISLAGRILAQ FPERLSDAQR
VSDDLAELGE LVHQPDANII KLPNISASLP QLRAAIAELQ AKGFDIPDYP EKPQNDEQRD
WQARYDRVKG SAVNPVLREG NSDRRAARAV KEYARKYPHS MGTWSPDSKS HVASMSSGDY
YESEKSTTVP AGGSATIRLL PESGDPITLR DGIILEAGEV IDAAVLRREE LRSYIAREIA
DAKKQGVLFS VHLKATMMKV SDPIIFGHFV SVFFADVFEK HAESFARLHI NPNNGLGDLL
SRITELPETE QQAIRDDIQD CLDNGPRVSM VDSDKGITNF HVPSDFIIDA TMPAAIRSSG
KSWSPEGNLE DTKFSIPDRC YAGVYQTVID DCKKHGAFDP TTMGSVANVG LMAQKAEEYG
SHDKTFEIQQ PGTVQVIDGS GAVLLEQTVA TGDIFRMCQV KDAAIRDWVR LAVERARLTG
SPAVFWLDAR RAHDAELIKK IEAYLPEHDT TGLELAVMAP AEATRYSVDR ARAGLDTISV
TGNVLRDYLT DLFPILELGT SAKMLSIVPL MNGGGLFETG AGGSAPKHVQ QFLQENHLRW
DSLGEFLALS VSFEHLGRVF SNDGARLLAD TLDAAVGQLL ENGKSPKRKV GELDNRGSHF
YIALYWARAM AEKAVGHALQ PAFATLADAL AEAEGAILQE LTECQGSPVD TGGYYRPATD
KASAAMRPSA TFNRILQEFT AGLHS
//
