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Database: UniProt
Entry: A0A085L877_9FIRM
LinkDB: A0A085L877_9FIRM
Original site: A0A085L877_9FIRM 
ID   A0A085L877_9FIRM        Unreviewed;       333 AA.
AC   A0A085L877;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:KFD41173.1};
DE            EC=1.1.1.41 {ECO:0000313|EMBL:KFD41173.1};
GN   ORFNames=DK28_0211600 {ECO:0000313|EMBL:KFD41173.1};
OS   Peptococcaceae bacterium SCADC1_2_3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD41173.1, ECO:0000313|Proteomes:UP000027084};
RN   [1] {ECO:0000313|EMBL:KFD41173.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41173.1};
RA   Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFD41173.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41173.1};
RA   Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT   "Draft genome sequence of an unculturable Firmicutes affiliated with
RT   Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT   degrading cultures.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFD41173.1}.
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DR   EMBL; JJNX02000053; KFD41173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085L877; -.
DR   STRING; 1487582.HY00_07435; -.
DR   Proteomes; UP000027084; 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   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;
KW   Oxidoreductase {ECO:0000313|EMBL:KFD41173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027084}.
FT   DOMAIN          4..328
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   333 AA;  35990 MW;  859D9A1978B66BF4 CRC64;
     MTYNVTLIPG DGIGPEISAA AKEIIDASGV NINWEVVLAG EAVMAEHRTP LPDYVLESIK
     RNRVALKGPI TTPVGGGFRS VNVTLRQKLN LYANVRPART LPGISTRYEK VDIIVVRENT
     EDLYAGIEHK VGKNAAESIK IITREASEKI VHFAFNLARR ESRKKVTAVH KANIMKLTDG
     LFLDCAREVA KDYPDISFDE MIVDALCMKL VQAPETYDVL VLPNLYGDIV SDLCAGLVGG
     LGVAPGANIG DDAAVFEPVH GSAPKHAGKN RVNPLAIILS GIMMLEHLNE KKAAQRVMEA
     VIAVLKEKTH LTYDLGGSAS TSEMAAAIIR KMS
//
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