LEU1A_SOLPN
ID LEU1A_SOLPN Reviewed; 589 AA.
AC O04973;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=2-isopropylmalate synthase A;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase A;
DE AltName: Full=Alpha-isopropylmalate synthase A;
GN Name=IPMSA;
OS Solanum pennellii (Tomato) (Lycopersicon pennellii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=28526;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Wei T., Maita D., Steffens J.C.;
RT "Cloning of two L. pennellii 2-isopropylmalate synthase cDNA and their
RT functional expression in yeast.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
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DR EMBL; AF004165; AAB61598.1; -; mRNA.
DR RefSeq; NP_001310380.1; NM_001323451.1.
DR AlphaFoldDB; O04973; -.
DR SMR; O04973; -.
DR GeneID; 107028537; -.
DR KEGG; spen:107028537; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS50991; PYR_CT; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Transferase.
FT CHAIN 1..589
FT /note="2-isopropylmalate synthase A"
FT /id="PRO_0000140446"
FT DOMAIN 48..321
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 589 AA; 64361 MW; 150E48900188BDDF CRC64;
MFFFLQLLVP IISVFQSKKH YYSTFIRCSI SNRRPEYVPS KISDPKYVRI FDTTLRDGEQ
SPGATMTTKE KLDVARQLAK LGVDIIEAGF PASSEADFES VKLIAEEIGN NTDENGFVPV
ICGLSRCNKS DIDKAWEAVK YAKKPRVHTF IATSEIHMKY KLKMSREQVV EKARSMVAYA
RSLGCEDVEF SPEDAGRSDR EFLYDILGEV IKAGATTLNI PDTVGYTVPS EFGQLITDIK
ANTPGIENVI ISTHCQNDLG LSTANTLAGA CAGARQLEVT INGIGERAGN ASLEEVVMAL
KCRGEQVLGG LYTGINTQHI VPSSKMVEEY SGLQVQPHKA IVGANAFAHE SGIHQDGMLK
HKDTYEIISP DDVGLSRSNE AGIVLGKLSG RHALKSKMLE LGYDIDGKEL EDLFWRFKSV
AEKKKKITDD DLIALMSDEV LQPNVYWKLG DVQIMCGSLG LSTATVKLIN TDGQEHIACS
VGTGPVDAAY KAVDLIVKVP ITLLEYSMNA VTEGIDAIAS TRVSICSIDR HTIMNGSTGQ
TIHRTFSGTG ADMDVVISSV RAYIGALNKM LSYEKLVSRY SKPEDSVVV
