ID A0A1E4RAS3_9BACI Unreviewed; 420 AA.
AC A0A1E4RAS3; A0A1H8F9Q1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BG258_16715 {ECO:0000313|EMBL:ODV57438.1}, SAMN02787113_01776
GN {ECO:0000313|EMBL:SEQ48031.1};
OS Lysinibacillus fusiformis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=28031 {ECO:0000313|EMBL:ODV57438.1, ECO:0000313|Proteomes:UP000094784};
RN [1] {ECO:0000313|EMBL:ODV57438.1, ECO:0000313|Proteomes:UP000094784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5 {ECO:0000313|EMBL:ODV57438.1,
RC ECO:0000313|Proteomes:UP000094784};
RA Gallegos-Monterrosa R., Maroti G., Balint B., Kovacs A.T.;
RT "Draft genome sequence of the soil isolate, Lysinibacillus fusiformis M5, a
RT potential hypoxanthine producer.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SEQ48031.1, ECO:0000313|Proteomes:UP000199410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-13 {ECO:0000313|EMBL:SEQ48031.1,
RC ECO:0000313|Proteomes:UP000199410};
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}.
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:ODV57438.1}.
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DR EMBL; MECQ01000001; ODV57438.1; -; Genomic_DNA.
DR EMBL; FOEL01000005; SEQ48031.1; -; Genomic_DNA.
DR RefSeq; WP_025114483.1; NZ_VEEI01000005.1.
DR AlphaFoldDB; A0A1E4RAS3; -.
DR GeneID; 29441561; -.
DR KEGG; lfu:HR49_06410; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000094784; Unassembled WGS sequence.
DR Proteomes; UP000199410; 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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 19..416
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 343..349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 356
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 399
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 149
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 219
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 89
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 231
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 420 AA; 46018 MW; 03C3C83D9557589B CRC64;
MSNKIVVENG VLNVPNNPVI PFIEGDGIGP DIWAAASRVI DAAVEKAYNG EKKIEWLEVL
AGEKAFNQTG EWLPQETLDK INEYLIAIKG PLTTPIGGGI RSLNVALRQQ LDLYVCLRPV
RHFDGVPSPV KRPEDVDMVI FRENTEDIYA GIEFESGSEQ AQKIINFLQS EFGVNQIRFP
ETSGIGVKPV SKEGTERLVR SAIEYAIKHK RPSVTLVHKG NIMKFTEGGF KKWGYELAEK
EFADQTFTWN QYDAIKAEQG EEAANKAQSD ALAAGKILVK DSIADIFLQQ ILTRPTEFDV
VATMNLNGDY ISDALAAQVG GIGIAPGANI NYVTGHAIFE ATHGTAPKYA GLDKVNPSSV
LLSGVLMLEH LGWQEAADMI TKSVENTISS KVVTYDFARL MDGATEVKCS EFANELIKNL
//
