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Database: UniProt
Entry: L8LT44_9CYAN
LinkDB: L8LT44_9CYAN
Original site: L8LT44_9CYAN 
ID   L8LT44_9CYAN            Unreviewed;       345 AA.
AC   L8LT44;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00019276};
DE            EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101};
DE   AltName: Full=3-IPM-DH {ECO:0000256|ARBA:ARBA00033138};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|ARBA:ARBA00030010};
GN   ORFNames=Xen7305DRAFT_00005450 {ECO:0000313|EMBL:ELS00844.1};
OS   Xenococcus sp. PCC 7305.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC   Xenococcus.
OX   NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS00844.1, ECO:0000313|Proteomes:UP000011203};
RN   [1] {ECO:0000313|EMBL:ELS00844.1, ECO:0000313|Proteomes:UP000011203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS00844.1,
RC   ECO:0000313|Proteomes:UP000011203};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00000624};
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   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004762}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008319}.
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:ELS00844.1}.
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DR   EMBL; ALVZ01000228; ELS00844.1; -; Genomic_DNA.
DR   RefSeq; WP_006511982.1; NZ_ALVZ01000228.1.
DR   AlphaFoldDB; L8LT44; -.
DR   STRING; 102125.Xen7305DRAFT_00005450; -.
DR   PATRIC; fig|102125.3.peg.4872; -.
DR   eggNOG; COG0473; Bacteria.
DR   OrthoDB; 9806254at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000011203; Unassembled WGS sequence.
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-UniPathway.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011203}.
FT   DOMAIN          6..339
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   345 AA;  38145 MW;  E868D6249BBBA612 CRC64;
     MNNQYRIAAL PGEGIGLEVV EATLVILQKL AQKHDFQLQI DYGVIGKSAF QKYGSYFPET
     TAQLCEQSDG ILFGAVSKGG LLELRKRFDF FVNLRPVKTF PSLIDKSSLK RDYLSGVDIL
     FVRELVSGIY FGAAGRGEDT QGNYGYHTMQ YYDWQIKRIA KVAFAKAQKR RGLLTVAHKE
     NALPYLPWTD LVAEVAQEYP DVTVEPMLVD NLAMQLVINP QHFDVILAGN LFGDILSDLG
     GALAGSVGLL GSASLNEAGF GLYEPIHGTA PDIAGKNQAN PLGTLASAMM MLEQWGERDA
     IANLQAAWNK ILTQGYRTRD LYSQEPEILV TTQELVELFL EEIEN
//
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