ID E1QP34_VULDI Unreviewed; 415 AA.
AC E1QP34;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN OrderedLocusNames=Vdis_2027 {ECO:0000313|EMBL:ADN51399.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN51399.1, ECO:0000313|Proteomes:UP000006681};
RN [1] {ECO:0000313|EMBL:ADN51399.1, ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX PubMed=21304741;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
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; CP002100; ADN51399.1; -; Genomic_DNA.
DR RefSeq; WP_013337124.1; NC_014537.1.
DR AlphaFoldDB; E1QP34; -.
DR STRING; 572478.Vdis_2027; -.
DR GeneID; 9752978; -.
DR KEGG; vdi:Vdis_2027; -.
DR eggNOG; arCOG01164; Archaea.
DR HOGENOM; CLU_031953_7_1_2; -.
DR OrthoDB; 23624at2157; -.
DR Proteomes; UP000006681; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADN51399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006681};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 28..407
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 335..341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 348
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 158
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 225
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 98
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 415 AA; 46498 MW; AEAB0E479E053F62 CRC64;
MSSRVKIPED GEPIVVQGGV WNVPNKPIIL YIEGDGIGPE ITNVAIKVIN KAVEKAYGSS
REIRWVKVYA GEEAERVYGN RFPEETINLI TRYRVVLKGP LETPIGGGWR SINVAIRMLL
DAYANVRPVK YMPGLESPLK HPERVDMVII RENTDDLYRG IEWSWDSPEA AKLRKFLKEE
LKIELEDDTG IGIKPISKFK TQRVARFAFK FAIENKRRSV TIMHKGNIMK YTEGAFREWA
YEVALKEFRE YIVTEEEVNK LYGGKVPPGK ILVNDRIADN MFQQIITRPE NYDVILAPNL
NGDYISDAAG ALIGDIGVLG GANVGDTGGM FEAVHGTAPK YAGKNVANPT GIIRAGELML
RFMGWREAAD LIDRAITEAI NQKKVTQDLA RYMGVQPLGT KEFGDALIEI IDQLK
//
