ID D3LVK6_9FIRM Unreviewed; 573 AA.
AC D3LVK6;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=HMPREF0889_1009 {ECO:0000313|EMBL:EFD93659.1};
OS Megasphaera genomosp. type_1 str. 28L.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=699218 {ECO:0000313|EMBL:EFD93659.1, ECO:0000313|Proteomes:UP000003242};
RN [1] {ECO:0000313|Proteomes:UP000003242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28L {ECO:0000313|Proteomes:UP000003242};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000064};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFD93659.1}.
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DR EMBL; ADGP01000021; EFD93659.1; -; Genomic_DNA.
DR RefSeq; WP_009369912.1; NZ_ADGP01000021.1.
DR AlphaFoldDB; D3LVK6; -.
DR STRING; 699218.HMPREF0889_1009; -.
DR eggNOG; COG0119; Bacteria.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000003242; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 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 Acyltransferase {ECO:0000313|EMBL:EFD93659.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 31..304
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 573 AA; 64117 MW; C9F2C8FF983F5AF9 CRC64;
MKTVQRYQKG YFLPPQTDWS WIRQEYPQQA PHWCSVDLRD GNQALVTPMC LEEKIAFYQM
LLRIGFKEIE VGFPAASETE YQFLRYLVTH DLIPEEVTIQ VLTQARENII KKTFAALKDV
PRAVVHVYNS TSLAQRQQVF RKSRREVKEL AVQGAELVRE WAEKTAGNFR FEYSPESFTG
TEPEYALEVC NAVLDVWQPS VERKAIINLP ATVEMSLPHV FAAQVAYMSR YLHYREATVL
SVHPHNDRGT GIAAAEMALL AGAERLEGTL FGNGERTGNV DLVTVAMNMK ALGVATQLDF
SFLPDIVSAY ETLTRMTVPP RQPYAGKLVF AAFSGSHQDA IVKGMHFRRE HPQAPWTCPY
LYIDPQSVGR TYDADVIRIN SQSGKGGVAF VLEEQYGLQI PKALREDFSY YIKGISDRQQ
RELQAAEIYQ LFRQRYEPHS DGMYVESFAV HKTGNRWQAK AVLVYGAEKQ VVEGVGNGQL
QAITNGICAA CGLDIADLVY SEHDLDGGTG SRGMAYIGIT DKTGITAWGI GVDTDTMTAA
VQAFTGAVQH HPVFSKQMSF QRRILSAIAV GGR
//
