ID T2SYX3_HELPX Unreviewed; 340 AA.
AC T2SYX3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
DE Flags: Fragment;
GN ORFNames=L933_08210 {ECO:0000313|EMBL:EQD97538.1};
OS Helicobacter pylori PZ5056.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1337393 {ECO:0000313|EMBL:EQD97538.1, ECO:0000313|Proteomes:UP000015834};
RN [1] {ECO:0000313|EMBL:EQD97538.1, ECO:0000313|Proteomes:UP000015834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PZ5056 {ECO:0000313|EMBL:EQD97538.1,
RC ECO:0000313|Proteomes:UP000015834};
RX PubMed=24051318;
RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT Regions of Low and High Gastric Cancer Risk in Colombia.";
RL Genome Announc. 1:e00736-13(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|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:EQD97538.1}.
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; ASYU01000137; EQD97538.1; -; Genomic_DNA.
DR AlphaFoldDB; T2SYX3; -.
DR Proteomes; UP000015834; 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:EQD97538.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 31..340
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT SITE 169
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 239
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 110
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT NON_TER 340
FT /evidence="ECO:0000313|EMBL:EQD97538.1"
SQ SEQUENCE 340 AA; 38180 MW; 38003A91B26880F4 CRC64;
MAYNPKILQK PKEGEEITIK DGKLHVPNYP IIPFIEGDGI GSDITPAMIK VVDSAVQKAY
KGEKKIAWYE VFVGEKCYQK FKDHKELSPE EQWLLPDTIE AINHYKVSIK GPLTTPIGEG
FRSLNVALRQ KMDLYVCLRP VRWYGSPSPV KEPQKVDMVI FRENSEDIYA GIEWQEGSAE
AKKLIHFLQN ELKVKKIRFP ESSGIGVKPI SKEGTERLVR KAIEYAIDND KPSVTFVHKG
NIMKYTEGAF MKWGYALAQK EFNAQVIDKG PWCSLKNPKT GKEIIIKDMI ADAFLQQILL
RPSEYSVIAT MNLNGDYISD ALAAMVGGIG IAPGANLNDT
//
