IDH_COXBU
ID IDH_COXBU Reviewed; 427 AA.
AC Q9ZH99; Q7C3F6; Q9RG62; Q9RG63; Q9RG64; Q9RG65; Q9RG66; Q9RG67; Q9RG68;
AC Q9RG69; Q9RG70; Q9RG71; Q9RG72;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Isocitrate dehydrogenase [NADP];
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; OrderedLocusNames=CBU_1200;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPTIMAL PH.
RC STRAIN=Nine Mile I;
RX PubMed=10361714; DOI=10.1111/j.1574-6968.1999.tb13607.x;
RA Van Nguyen S., To H., Yamaguchi T., Fukushi H., Hirai K.;
RT "Molecular cloning of an immunogenic and acid-induced isocitrate
RT dehydrogenase gene from Coxiella burnetii.";
RL FEMS Microbiol. Lett. 175:101-106(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1M, 27M, 307, 3M, 605, 60M, 82M, Bangui VR 730, El Tayeb RSA 342,
RC GQ212, KoQ229, MAN, ME, Ohio 314 VR 542, Priscilla, SQ217, and TK-1;
RX PubMed=10556719; DOI=10.1111/j.1574-6968.1999.tb08803.x;
RA Nguyen S.V., Hirai K.;
RT "Differentiation of Coxiella burnetii isolates by sequence determination
RT and PCR-restriction fragment length polymorphism analysis of isocitrate
RT dehydrogenase gene.";
RL FEMS Microbiol. Lett. 180:249-254(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(2007).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.7.;
CC -!- DEVELOPMENTAL STAGE: Detected in both the small cell variant (SCV) and
CC in the large cell variant (LCV) stage (at protein level). LCVs are more
CC metabolically active than SCVs. {ECO:0000269|PubMed:17088354}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO90709.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF069035; AAC68600.1; -; Genomic_DNA.
DR EMBL; AF146284; AAF16725.1; -; Genomic_DNA.
DR EMBL; AF146285; AAF16726.1; -; Genomic_DNA.
DR EMBL; AF146286; AAF16727.1; -; Genomic_DNA.
DR EMBL; AF146287; AAF16728.1; -; Genomic_DNA.
DR EMBL; AF146288; AAF16729.1; -; Genomic_DNA.
DR EMBL; AF146289; AAF16730.1; -; Genomic_DNA.
DR EMBL; AF146290; AAF16731.1; -; Genomic_DNA.
DR EMBL; AF146291; AAF16732.1; -; Genomic_DNA.
DR EMBL; AF146292; AAF16733.1; -; Genomic_DNA.
DR EMBL; AF146293; AAF16734.1; -; Genomic_DNA.
DR EMBL; AF146294; AAF16735.1; -; Genomic_DNA.
DR EMBL; AF146295; AAF16736.1; -; Genomic_DNA.
DR EMBL; AF146296; AAF16737.1; -; Genomic_DNA.
DR EMBL; AF146297; AAF16738.1; -; Genomic_DNA.
DR EMBL; AF146298; AAF16739.1; -; Genomic_DNA.
DR EMBL; AF146299; AAF16740.1; -; Genomic_DNA.
DR EMBL; AF146300; AAF16741.1; -; Genomic_DNA.
DR EMBL; AF146301; AAF16742.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90709.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_820195.2; NC_002971.3.
DR AlphaFoldDB; Q9ZH99; -.
DR SMR; Q9ZH99; -.
DR STRING; 227377.CBU_1200; -.
DR PRIDE; Q9ZH99; -.
DR EnsemblBacteria; AAO90709; AAO90709; CBU_1200.
DR GeneID; 1209104; -.
DR KEGG; cbu:CBU_1200; -.
DR PATRIC; fig|227377.7.peg.1195; -.
DR eggNOG; COG0538; Bacteria.
DR HOGENOM; CLU_031953_7_1_6; -.
DR OMA; CVRPCRY; -.
DR Proteomes; UP000002671; Chromosome.
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 Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..427
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000323713"
FT BINDING 114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 349..355
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 240
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT VARIANT 20
FT /note="Q -> E (in strain: GQ212, KoQ229, SQ217)"
FT VARIANT 32
FT /note="E -> V (in strain: TK-1)"
FT VARIANT 33
FT /note="V -> A (in strain: GQ212)"
FT VARIANT 52
FT /note="A -> T (in strain: GQ212, KoQ229, MAN, ME,
FT Priscilla, SQ217)"
FT VARIANT 63
FT /note="V -> A (in strain: ME)"
FT VARIANT 87
FT /note="V -> A (in strain: SQ217)"
FT VARIANT 100
FT /note="E -> G (in strain: California 76 VR 614)"
FT VARIANT 104
FT /note="E -> G (in strain: 605)"
FT VARIANT 183
FT /note="V -> M (in strain: Priscilla)"
FT VARIANT 271
FT /note="G -> R (in strain: Bangui VR 730)"
FT VARIANT 306
FT /note="Y -> C (in strain: Bangui VR 730)"
FT VARIANT 379
FT /note="W -> R (in strain: El Tayeb RSA 342)"
FT VARIANT 415
FT /note="T -> A (in strain: GQ212, KoQ229, SQ217)"
FT VARIANT 419
FT /note="G -> A (in strain: GQ212, KoQ229, SQ217)"
SQ SEQUENCE 427 AA; 46636 MW; E23462962C26C138 CRC64;
MTELTGVSIV TYQHIKVPSQ GEKITVNKAV LEVPDRPIIP FIEGDGIGID IAPVMKNVVD
AAVEKSYAGK RKIEWMEIYA GEKATKVYGK DNWLPDETLE AIKEYQVAIK GPLTTPVGGG
IRSLNVALRQ QLDLYVCLRP VRYFTGVPSP VKTPEKVNMV IFRENSEDIY AGIEWPAGSP
EAVKLINFLQ NEMGVKKIRF PETAGIGIKP VSKEGTSRLV RRAIQYAIDN DRDSVTLVHK
GNIMKFTEGA FKDWGYEVAV KEFGAKPLDG GPWHVFENPK TGQKITIKDV IADAFLQQIL
LRPAEYSVIA TLNLNGDYIS DALAAEVGGI GIAPGANLSD TVGLFEATHG TAPKYAGQDK
VNPGSLILSA EMMLRYLGWK EAADLVVQGI EGAIESKTVT YDFARLMTGA KEVSTSQFGK
AIIKHIL
