IDH_PSEAB
ID IDH_PSEAB Reviewed; 418 AA.
AC Q02NB5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000255|RuleBase:RU004446};
DE Short=IDH;
DE EC=1.1.1.42 {ECO:0000255|RuleBase:RU004446};
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; OrderedLocusNames=PA14_30190;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-115.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-115 AND THR-193.
RC STRAIN=UCBPP-PA14;
RX PubMed=24965220; DOI=10.1002/pmic.201400190;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT aeruginosa PA14 strain.";
RL Proteomics 14:2017-2030(2014).
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:0000255|RuleBase:RU004446};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08200};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P08200};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08200}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
CC Note=Could be present extracellularly due to cell lysis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000255|RuleBase:RU004443}.
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DR EMBL; CP000438; ABJ11846.1; -; Genomic_DNA.
DR RefSeq; WP_003090436.1; NZ_CP034244.1.
DR PDB; 5M2E; X-ray; 2.70 A; A/B/C/D=1-418.
DR PDBsum; 5M2E; -.
DR AlphaFoldDB; Q02NB5; -.
DR SMR; Q02NB5; -.
DR iPTMnet; Q02NB5; -.
DR PRIDE; Q02NB5; -.
DR EnsemblBacteria; ABJ11846; ABJ11846; PA14_30190.
DR KEGG; pau:PA14_30190; -.
DR HOGENOM; CLU_031953_7_1_6; -.
DR OMA; CVRPCRY; -.
DR BioCyc; PAER208963:G1G74-2528-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; PTHR43504; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glyoxylate bypass; Magnesium; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Secreted; Tricarboxylic acid cycle.
FT CHAIN 1..418
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000431337"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT SITE 162
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT SITE 232
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24965220,
FT ECO:0000269|PubMed:25096199"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24965220"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 40..59
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:5M2E"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5M2E"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5M2E"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:5M2E"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 372..387
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:5M2E"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:5M2E"
SQ SEQUENCE 418 AA; 45577 MW; 157FF37CF02EC20A CRC64;
MGYQKIQVPA TGDKITVNAD MSLSVPKNPI IPFIEGDGIG VDISPVMIKV VDAAVEKAYK
GERKIAWMEV YAGEKATQVY DQDTWLPQET LDAVRDYVVS IKGPLTTPVG GGIRSLNVAL
RQQLDLYVCQ RPVRWFEGVP SPVKKPGDVD MVIFRENSED IYAGVEWKAG SPEAEKVIKF
LTEEMGVKKI RFTENCGIGI KPVSQEGTKR LVRKALQYAV DNDRSSVTLV HKGNIMKFTE
GAFKDWGYEV ARDEFGAELL DGGPWMQFKN PKTGKNVVVK DVIADAMLQQ ILLRPAEYDV
IATLNLNGDY LSDALAAEVG GIGIAPGANL SDSVAMFEAT HGTAPKYAGQ DKVNPGSLIL
SAEMMLRHMG WTEAADLIIK GTNGAIAAKT VTYDFERLMD GATLLSCSEF GDAMIAKM
