LEU1B_SOLPN
ID LEU1B_SOLPN Reviewed; 612 AA.
AC O04974;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=2-isopropylmalate synthase B;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase B;
DE AltName: Full=Alpha-isopropylmalate synthase B;
GN Name=IPMSB;
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; AF004166; AAB61599.1; -; mRNA.
DR RefSeq; NP_001310373.1; NM_001323444.1.
DR AlphaFoldDB; O04974; -.
DR SMR; O04974; -.
DR GeneID; 107023302; -.
DR KEGG; spen:107023302; -.
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..612
FT /note="2-isopropylmalate synthase B"
FT /id="PRO_0000140447"
FT DOMAIN 71..344
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 612 AA; 66535 MW; 2EC5AECC9039791B CRC64;
MASITANHPI SGKPLISFRP KNPLLQTQTL FNFKPSISKH SNSSFSIPVV RCSIRRIPEY
TPSHIPDPNY VRIFDTTLRD GEQSPGATMT TKEKLDVARQ SAKLGVDIIE AGFPASSEAD
LEAVKLIAKE VGNGVYEEEY VPVICGLARC NKKDIDKAWE AVKYAKKPRI HTFIATSEVH
MNYKLKMSRD QVVEKARSMV AYARSIGCED VEFSPEDAGR SDPEFLYHIL GEVIKAGATT
LNIPDTVGYT VPEEFGQLIA KIKANTPGVE DVIISTHCQN DLGLSTANTL AGACAGARQL
EVTINGIGER AGNASLEEVV MALKCRGEQV LGGLYTGINT QHILMSSKMV EGISGLHVQP
HKAIVGANAF VHESGIHQDG MLKHKDTYEI ISPEDIGLNR ANESGIVFGK LSGVMLCKPK
MLELGYEIEG KELDDLFWRF KSVAEKKKKI TDDDLVALMS DEVFQPQFVW QLQNVQVTCG
SLGLSTATVK LIDADGREHI SCSVGTGPVD AAYKAVDLIV KVPVTLLEYS MNAVTQGIDA
IASTRVLIRG ENGHTSTHAL TGETVHRTFS GTGADMDIVI SSVRAYVGAL NKMMSFRKLM
AKNNKPESSA VI
