ID A0A136JN36_9BACT Unreviewed; 414 AA.
AC A0A136JN36;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Isocitrate dehydrogenase, NAD-dependent, mitochondrial type {ECO:0000313|EMBL:KXJ98565.1};
DE EC=1.1.1.41 {ECO:0000313|EMBL:KXJ98565.1};
GN ORFNames=UZ17_ACD001002634 {ECO:0000313|EMBL:KXJ98565.1};
OS Acidobacteria bacterium OLB17.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1617423 {ECO:0000313|EMBL:KXJ98565.1, ECO:0000313|Proteomes:UP000070331};
RN [1] {ECO:0000313|EMBL:KXJ98565.1, ECO:0000313|Proteomes:UP000070331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB17 {ECO:0000313|EMBL:KXJ98565.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXJ98565.1}.
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DR EMBL; LLEU01000059; KXJ98565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JN36; -.
DR STRING; 1617423.UZ17_ACD001002634; -.
DR PATRIC; fig|1617423.3.peg.2754; -.
DR Proteomes; UP000070331; Unassembled WGS sequence.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) 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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KXJ98565.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 49..373
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 414 AA; 44613 MW; 78561B52ADC4D9EB CRC64;
MQSYGVAELR SAALPVTPAL CNSETLPTSP NSFVTSTPPS HNIGFMKHTI TLIPGDGIGP
EIVAATVRVI EATGVDIEWE TQILGAQAQE KYGTTLPDGT IDSIKQNKVA LKGPQMTPVG
KGFTSVNVGL RKALDLYANV RPVKALPNVP CRYPELDLVI VRENTEDLYA GLEHVVVPGV
VESLKIITEK ASTRIARYAF EYAKANGRKK VTAVHKANIM KLSDGLFLEC FYGVAKDFPE
IEADDKIIDN CCMQLVMRPE QFDVLVLENL YGDIVSDLCA GLIGGLGLAP GANIGELGAV
FEAVHGSAPD IAGQGIANPT ALMLSAVQML HHIGEKEAAD RMNNAMLAVF ADGKTLTRDL
GGTAKTNEFA RAIVEKFRPK QLPRPDLRIF FRRASAVLLS VSVYQTRTRS LGAR
//
