ID A0A0F7HLP2_9STAP Unreviewed; 421 AA.
AC A0A0F7HLP2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562, ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013, ECO:0000256|RuleBase:RU004446};
GN ORFNames=AAT16_08320 {ECO:0000313|EMBL:AKG74237.1}, SAMN05216235_2559
GN {ECO:0000313|EMBL:SFK93401.1};
OS Salinicoccus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG74237.1, ECO:0000313|Proteomes:UP000034029};
RN [1] {ECO:0000313|EMBL:AKG74237.1, ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|EMBL:AKG74237.1,
RC ECO:0000313|Proteomes:UP000034029};
RX PubMed=26634017;
RA Jiang K., Xue Y., Ma Y.;
RT "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT the Qaidam Basin in China.";
RL Stand. Genomic Sci. 10:116-116(2015).
RN [2] {ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA Ma Y., Jiang K., Xue Y.;
RT "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT from the Qaidam basin of China.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFK93401.1, ECO:0000313|Proteomes:UP000183090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6501 {ECO:0000313|EMBL:SFK93401.1,
RC ECO:0000313|Proteomes:UP000183090};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR604439-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; CP011366; AKG74237.1; -; Genomic_DNA.
DR EMBL; FOTB01000006; SFK93401.1; -; Genomic_DNA.
DR RefSeq; WP_046790419.1; NZ_FOTB01000006.1.
DR AlphaFoldDB; A0A0F7HLP2; -.
DR STRING; 407035.AAT16_08320; -.
DR KEGG; shv:AAT16_08320; -.
DR PATRIC; fig|407035.3.peg.1722; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000034029; Chromosome.
DR Proteomes; UP000183090; Unassembled WGS sequence.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00183; prok_nadp_idh; 1.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU004446};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004446};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AKG74237.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 20..417
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 94
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 344..350
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 357
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 150
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 220
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 232
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 421 AA; 46290 MW; 4CC0E780F4EFD2E9 CRC64;
MSSSKITTDN GVLNVPDNPV IPFIEGDGIG PDIWSAASKV LDAAVEKAYN GEKKIEWKEV
LAGQKAFDKT GEWLPKETLD TIDEYLLAIK GPLTTPIGGG IRSLNVALRQ ELDLFTCLRP
VRYFDGVPSP IKRPEDTDMV IFRENTEDIY AGIEFQEGTD EVKKVIDFLQ NEMGAKNIRF
PETSGIGIKP VSKEGTERLV RSAINYAIDN NRPSVTLVHK GNIMKFTEGA FKAWGYDLAE
REFGDKVFTW KEYDKIVEEK GREEADKVQG EAEASGKIII KDAIADIFLQ QILTRPKDFG
VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLDKVNPSS
VVLSGVLMLE HLGWQEAADL VTKAMEKTIA SKVVTYDFAR LMDNAKEVKC SEFGNELIKN
M
//
