ID A0A0S8DMC1_9BACT Unreviewed; 358 AA.
AC A0A0S8DMC1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:KPK36881.1};
GN ORFNames=AMK70_00655 {ECO:0000313|EMBL:KPK36881.1};
OS Nitrospira bacterium SG8_35_1.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK36881.1, ECO:0000313|Proteomes:UP000052010};
RN [1] {ECO:0000313|EMBL:KPK36881.1, ECO:0000313|Proteomes:UP000052010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK36881.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK36881.1}.
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DR EMBL; LJTK01000004; KPK36881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DMC1; -.
DR PATRIC; fig|1704024.3.peg.521; -.
DR Proteomes; UP000052010; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
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;
FT DOMAIN 3..353
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 358 AA; 39198 MW; 080F880C6D22A306 CRC64;
MYRVTLIPGD GTGPEITEAA VRVLEATGVK FDWDIQNAGE DVYHDEGNPL PERVLASIKK
NKVAIKGPIT TPVGTGFRSV NVTLRQTLDL YSCVRPCKTY KGAKTRYENL DLVIFRENTE
DLYAGIEYQK DSEGARAIID LVKKLSDRSI RPDSGISIKP ISVYGTERIV RAAFEYAQKN
ARRKVTAVHK ANIMKYSDGL FLEVSREVAK DYPDIEFEDK IIDNMCMQLV QKPELYDILV
LPNLYGDVVS DLAAGLIGGL GLAPGANIGD EYAVFEATHG SAPKYKGLNK VNPLAVILSG
IMMLRYLGEV EAAEKLDSAV SAVIEEGRNV TYDMKPTPDD PSAATTSGMA DAIIGKLR
//
