ID C1F3J9_ACIC5 Unreviewed; 502 AA.
AC C1F3J9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE AltName: Full=IDP {ECO:0000256|ARBA:ARBA00029765};
DE AltName: Full=NADP(+)-specific ICDH {ECO:0000256|ARBA:ARBA00029990};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|ARBA:ARBA00031098};
GN Name=icd2 {ECO:0000313|EMBL:ACO34160.1};
GN OrderedLocusNames=ACP_0990 {ECO:0000313|EMBL:ACO34160.1};
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO34160.1, ECO:0000313|Proteomes:UP000002207};
RN [1] {ECO:0000313|EMBL:ACO34160.1, ECO:0000313|Proteomes:UP000002207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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|ARBA:ARBA00001946};
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; CP001472; ACO34160.1; -; Genomic_DNA.
DR AlphaFoldDB; C1F3J9; -.
DR STRING; 240015.ACP_0990; -.
DR KEGG; aca:ACP_0990; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_1_0_0; -.
DR InParanoid; C1F3J9; -.
DR Proteomes; UP000002207; 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:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.70.1570; -; 1.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR014273; Isocitrate_DH_bac-typ.
DR InterPro; IPR040978; Isocitrate_DH_TT1725_C.
DR InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR02924; ICDH_alpha; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF43; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR Pfam; PF18324; Isocitrate_DH_C_bact; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACO34160.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002207}.
FT DOMAIN 23..352
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT REGION 367..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 54435 MW; D64DE54F9942C9E5 CRC64;
MHSPSTDLEQ AELAQDSKLT PIPVTVAAGD GIGPEITAAV MSILSAAGAH LDAEYVEVGE
QVYLRGNTSG IPQEAWDSIA RTRVMLKGPI TTPQGGGYKS LNVTMRKTLG LYANVRPCRT
YKPIVTTRHP DMDVVIVREN EEDLYAGIEH RQTQDVAQCL KLITRSGSER IARYAFEYAR
QHGRSKITCM IKDNIMKLTD GLFHRVFDEV AREYPEIQAH SQIVDFGMAN FVHRPEDYDV
VLLPNLYGDI LSDIAAQMTG SVGLGGSVNI GSGGAIFEAI HGSAPDLARD VANPSGLLLA
AVEMLRHLKL DSIAAKVMNA WLCTLEEGIH TVDIAGAHTK ERAGTRRFTE AVIERLGRRP
VQLAAVDEPA TQSTEPLETG VSANPTSVLN TPVEKKTLVG VDVFVDEAGV LPDALAAKLQ
AASTGEFTLK MITNRGVKVW PNGREETLCT DHWRCRFEGA NPRNADVAGL LANLAHAGID
FIKTEQLYNF DGKPGYSLGQ GQ
//
