ID L7VK61_9FLAO Unreviewed; 350 AA.
AC L7VK61;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 13-SEP-2023, entry version 51.
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};
GN Name=leuB {ECO:0000313|EMBL:AGC66866.1};
GN ORFNames=ASNER_098 {ECO:0000313|EMBL:AGC66866.1};
OS Candidatus Uzinura diaspidicola str. ASNER.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Candidatus Uzinura.
OX NCBI_TaxID=1133592 {ECO:0000313|EMBL:AGC66866.1, ECO:0000313|Proteomes:UP000011174};
RN [1] {ECO:0000313|EMBL:AGC66866.1, ECO:0000313|Proteomes:UP000011174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASNER {ECO:0000313|EMBL:AGC66866.1,
RC ECO:0000313|Proteomes:UP000011174};
RX PubMed=23279075; DOI=10.1111/1462-2920.12058;
RA Sabree Z.L., Huang C.Y., Okusu A., Moran N.A., Normark B.B.;
RT "The nutrient supplying capabilities of Uzinura, an endosymbiont of
RT armoured scale insects.";
RL Environ. Microbiol. 15:1988-1999(2013).
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; CP003263; AGC66866.1; -; Genomic_DNA.
DR AlphaFoldDB; L7VK61; -.
DR STRING; 1133592.ASNER_098; -.
DR KEGG; udi:ASNER_098; -.
DR PATRIC; fig|1133592.3.peg.86; -.
DR HOGENOM; CLU_031953_0_3_10; -.
DR OrthoDB; 9806254at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000011174; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011174}.
FT DOMAIN 4..345
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 350 AA; 39253 MW; 4254DA4CE68AC0C0 CRC64;
MIKKIAILSG DGVGDEITTQ SLKVLNAIGK KFHHDFLYQE GLIGAIAIDN SGKPLPDDTL
SICIDSDAIL FGAIGDPKYD QDPCSKIRPE KGLLNIRRVL NIFCNIRPIM TYDALLKRSP
LNTERVKGID FLVYRELIGG IYFGDKGIYE DKKAYDYCFY SIEEIQRIGH IAFKAAIARH
KKLTLVDKAN VLETSRLWRE TIQTMAKDYS NVEVDFLFID NAAMQILLHP KNFDVILTDN
MFGDILSDEA SVISGSIGLS PSASIGDKNA LFEPIHGSYY QAARKNIANP LASILSVAMM
LDYFKLEKEA QLVRKAVYNS INYRKSSFDI SYFYPIGTEE VGDFIVQELS
//
