LEU1_HAEIN
ID LEU1_HAEIN Reviewed; 515 AA.
AC P43861;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=HI_0986;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7768823; DOI=10.1128/jb.177.11.3235-3240.1995;
RA Karudapuram S., Zhao X., Barcak G.J.;
RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a gene
RT required for chromosomal but not plasmid DNA transformation.";
RL J. Bacteriol. 177:3235-3240(1995).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22647.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18657; AAA70115.1; -; Genomic_DNA.
DR PIR; E64106; E64106.
DR RefSeq; NP_439149.2; NC_000907.1.
DR RefSeq; WP_005693326.1; NC_000907.1.
DR AlphaFoldDB; P43861; -.
DR SMR; P43861; -.
DR STRING; 71421.HI_0986; -.
DR EnsemblBacteria; AAC22647; AAC22647; HI_0986.
DR KEGG; hin:HI_0986; -.
DR PATRIC; fig|71421.8.peg.1029; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_6; -.
DR PhylomeDB; P43861; -.
DR BioCyc; HINF71421:G1GJ1-1028-MON; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..515
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140355"
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 515 AA; 56081 MW; 4521713EEE974792 CRC64;
MTDRVIIFDT TLRDGEQALK ASLTVKEKLQ IALALERLGV DVMEVGFPVS SQGDFESVQT
IARHIKNARV AALSRAVDKD IDAAYEALKV AEAFRIHTFI ASSALHVEAK LKRSFDDVVG
MAVAAVKRAR NYTDDVEFSC EDAGRTGIDN ICRIVEAAIN AGATTVNIPD TVGFCLPNEY
GNIIAQVRNC VPNIDKAVIS VHCHNDLGMA TANSLTAVQN GARQIECTIN GIGERAGNTS
LEEVVMAMKV RQDFMGVDTH INTQEIHRVS QMVSQLCNMP IQPNKAIVGS NAFAHSSGIH
QDGMLKNKNT YEILSPETIG LKKEKLNLTA RSGRAAVKGH MADMGYNEQD YDLDKLYDEF
LKLADKKGQV FDYDLEALAF IDMQQGDEDR LVLDKLSAHS TKEYPATAFV QLKLDGEKLS
TSSIGGNGPV DAVYNAILNL TGLEIKMSHY NLTAKGEGAE ALGQVDIVVE HKGRKFHGVG
LATDIVESSA LALVHAINAI YRAHKVADIK NHKHH
