ID   H5SKP6_9ZZZZ            Unreviewed;       369 AA.
AC   H5SKP6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:BAL56732.1};
GN   ORFNames=HGMM_F42E07C34 {ECO:0000313|EMBL:BAL56732.1};
OS   uncultured prokaryote.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=198431 {ECO:0000313|EMBL:BAL56732.1};
RN   [1] {ECO:0000313|EMBL:BAL56732.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL56732.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; AP011756; BAL56732.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SKP6; -.
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          12..359
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   369 AA;  39525 MW;  B3C67DE84E257C92 CRC64;
     MSSSGPRQAA YRLGVLKGDG IGPEVVPVAV DLADLSAHAA GLSVEWVELP VGLEAYGQLG
     DTLPQQTVEA LHGCHGWVLG PVEHHRYRLG MRNPSGTLRR LFDLYANERP ARNLPAVPSR
     YEAVDLVVVR ENTEGFYADR NVLEGDAEVL VTPDVVISLR VVTRRACERI AEYAFQLARR
     RARLRARPGR VTAVHKANVL RRGDGLFLAC CRAVASRYPD VAFDHVHVDA AAYFLVRDPQ
     RYDVLVTTNL FGDILSDQAA GLVGSLGVAP SLNAGDEHAM AQAVHGSAPD VAGSGVANPT
     AEILSLAMLF EWLGRRFDDP AATEAARRLE EAVGAALSAG VRTPDLGGSA TTAEFARAVR
     ARLSPGSML
//