ID Q200V9_STAAU Unreviewed; 283 AA.
AC Q200V9;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 13-SEP-2023, entry version 89.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00019276, ECO:0000256|RuleBase:RU004445};
DE EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
DE Flags: Fragment;
GN Name=leuB {ECO:0000313|EMBL:ABD73577.1};
OS Staphylococcus aureus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:ABD73577.1};
RN [1] {ECO:0000313|EMBL:ABD73577.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D22 {ECO:0000313|EMBL:ABD73577.1};
RX PubMed=16622047; DOI=10.1099/mic.0.28620-0;
RA Cooper J.E., Feil E.J.;
RT "The phylogeny of Staphylococcus aureus -- which genes make the best intra-
RT species markers?";
RL Microbiology 152:1297-1305(2006).
CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC {ECO:0000256|RuleBase:RU004445}.
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 ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|RuleBase:RU004445};
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. {ECO:0000256|ARBA:ARBA00004762,
CC ECO:0000256|RuleBase:RU004445}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004445}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008319}.
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DR EMBL; DQ413515; ABD73577.1; -; Genomic_DNA.
DR AlphaFoldDB; Q200V9; -.
DR UniPathway; UPA00048; UER00072.
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 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 ECO:0000256|RuleBase:RU004445};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW ECO:0000256|RuleBase:RU004445}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004445};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004445};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004443}.
FT DOMAIN 1..283
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD73577.1"
FT NON_TER 283
FT /evidence="ECO:0000313|EMBL:ABD73577.1"
SQ SEQUENCE 283 AA; 31136 MW; 6BA7746D0F1B0C90 CRC64;
EIISNKYNFN YQIEHHEFGG ASIDTFGEPL TEKTLNACKR ADAILLGAIG GPNWTDPNNR
PEQGLLKLRK SLNLFANIRP TTVVKGASSL SPLKQERVEG TDLVIVRELT SGIYFGEPRH
FNNHEALDSL TYTREEIERI VHVAFKLAAS RRGKLTSVDK ENVLASSKLW RKVVNEVSQL
YPEVTVNHLL VDACSMHLIT NPKQFDVIVC ENLFGDILSD EASVIPGSLG LSPSASFSND
GPRLYEPIHG SAPDIAGKNV ANPFGMILSL AMCLRESLNQ PDA
//
