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Database: UniProt
Entry: X1F4L7_9ZZZZ
LinkDB: X1F4L7_9ZZZZ
Original site: X1F4L7_9ZZZZ 
ID   X1F4L7_9ZZZZ            Unreviewed;       364 AA.
AC   X1F4L7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00013101};
DE            EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101};
GN   ORFNames=S03H2_16326 {ECO:0000313|EMBL:GAH39892.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAH39892.1};
RN   [1] {ECO:0000313|EMBL:GAH39892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAH39892.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(2014).
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:GAH39892.1}.
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DR   EMBL; BARU01008334; GAH39892.1; -; Genomic_DNA.
DR   AlphaFoldDB; X1F4L7; -.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase 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:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   NCBIfam; TIGR00169; leuB; 1.
DR   PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          4..358
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   364 AA;  39869 MW;  F4D023266315DB69 CRC64;
     MQIDLAVLPG DGIGPEVASE AIKVLQAVGD RFGHNFNLHY GLVGGIAIDQ SGTALSSDTL
     KMCRGCRAVL LGAVGGPKWD DPKAKVRPED GLLALRKELG LFANLRPVRV FPVLVDSTNL
     KPEVIQGVDF IFVRELTGGL YFARPKRQWQ TSRGRRATDS MTYSEQEIER IIRVGFELAR
     GRGKKLVSVD KANVLEVSRL WRQVAIEVAE EYPDVELEHM LVDACAMRLI QNPAYFDVIV
     TENMFGDILT DEASMLAGSM GMLPSASLAG VPREGVNIFG MYEPIHGSAP RRAGLNMANP
     MAIILSVAMM LRYSFGLEKE AQAIEAAVDK VLQQGYRTYD IMSQGKTRLG TKEMGELIAR
     QIGG
//
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