LEU1_RHOBA
ID LEU1_RHOBA Reviewed; 527 AA.
AC Q7UI51;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=RB12756;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000255|HAMAP-
CC Rule:MF_01025}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_01025}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD77763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294155; CAD77763.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_870686.1; NC_005027.1.
DR AlphaFoldDB; Q7UI51; -.
DR SMR; Q7UI51; -.
DR STRING; 243090.RB12756; -.
DR EnsemblBacteria; CAD77763; CAD77763; RB12756.
DR KEGG; rba:RB12756; -.
DR PATRIC; fig|243090.15.peg.6183; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_0; -.
DR InParanoid; Q7UI51; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001025; 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..527
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140373"
FT DOMAIN 18..280
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 527 AA; 57350 MW; 87C6FFCD04409329 CRC64;
MNQSAEAPSS ENVATRQIRI FDTTLRDGEQ SPGASMNLAE KLEVASALVD LGVDIIEAGF
PIASPGDFES VRQIATTIRG ATICGLARCA EKDIDRAWEA LKTAPQARIH VFLATSAIHR
EFKLRMTPDE IVERAVAGVR RAASHCDDVE FSPEDACRTE HDFLCRVVEA AIDAGATTIN
VPDTVGYTTP GEIYDRFKML RDRVPNMDKA VLSTHCHDDL GMAVANSLAA VDAGAGQIEC
TINGIGERAG NAALEELVMA MKTRQDFYHC QTNINSKRLV PVSRLVSKTT GINVQRNKAI
VGRNAFAHES GIHQDGMLKE RTTYEIMSPE EVGFTKTDLV LGKHSGRAAL ADRAKQLGMT
LTGEQLQEVF EAFKELADKK KEIYDGDIVA LVQQKISETV APEWTLVDYE VTSGKNQTPN
VRVTLRRDEQ DITEQVAQGD GPIDAAFWAV EKITGIQVVC KDFRVRSATL GRDAIGEVNL
EVEHEGKTYR GTGVSTDSVE STILAMLNAI NRIVAGIASD PGELPQP
