ID A0A2K9E1G6_9FIRM Unreviewed; 509 AA.
AC A0A2K9E1G6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198, ECO:0000256|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN Name=leuA1 {ECO:0000313|EMBL:AUG56208.1};
GN Synonyms=leuA {ECO:0000256|HAMAP-Rule:MF_01025};
GN ORFNames=B9R14_01705 {ECO:0000313|EMBL:PQQ65605.1}, HVS_01190
GN {ECO:0000313|EMBL:AUG56208.1};
OS Acetivibrio saccincola.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1677857 {ECO:0000313|EMBL:AUG56208.1, ECO:0000313|Proteomes:UP000233534};
RN [1] {ECO:0000313|EMBL:AUG56208.1, ECO:0000313|Proteomes:UP000233534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GGR1 {ECO:0000313|EMBL:AUG56208.1}, and SR1
RC {ECO:0000313|Proteomes:UP000233534};
RA Pechtl A., Ruckert C., Koeck D.E., Maus I., Winkler A., Kalinowski J.,
RA Puhler A., Schwarz W.W., Zverlov V.V., Schluter A., Liebl W.;
RT "Complete genome sequence of Herbivorax saccincola GGR1, a novel
RT Cellulosome-producing hydrolytic bacterium in a thermophilic biogas plant,
RT established by Illumina and Nanopore MinION sequencing.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQQ65605.1, ECO:0000313|Proteomes:UP000239720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:PQQ65605.1,
RC ECO:0000313|Proteomes:UP000239720};
RX PubMed=29482868; DOI=10.1016/j.syapm.2018.01.010;
RA Aikawa S., Baramee S., Sermsathanaswadi J., Thianheng P., Tachaapaikoon C.,
RA Shikata A., Waeonukul R., Pason P., Ratanakhanokchai K., Kosugi A.;
RT "Characterization and high-quality draft genome sequence of Herbivorax
RT saccincola A7, an anaerobic, alkaliphilic, thermophilic, cellulolytic, and
RT xylanolytic bacterium.";
RL Syst. Appl. Microbiol. 41:261-269(2018).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01025};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000256|ARBA:ARBA00004689,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
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DR EMBL; CP025197; AUG56208.1; -; Genomic_DNA.
DR EMBL; NEMB01000003; PQQ65605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9E1G6; -.
DR KEGG; hsc:HVS_01190; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000233534; Chromosome.
DR Proteomes; UP000239720; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00973; leuA_bact; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 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 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:AUG56208.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01025};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01025};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01025}; Reference proteome {ECO:0000313|Proteomes:UP000233534};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01025}.
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 392..509
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 204
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ SEQUENCE 509 AA; 55605 MW; 2367A70146A1059B CRC64;
MSRRIKIFDT TLRDGEQTPG VNLNINEKLE IAKQLERLGV DVIEAGFAIA SPGDFKAVKA
VAENVKNATV ASLARALEKD IDRAWEAVKE AENPLIHTFI ATSDIHLKYK LKMTEEEVLE
RAVAMVKYAK KYCSHVEFSA EDASRTRPEF LFKVLEKVID AGAVVVNIPD TVGYATPIEF
GNLIKAIKEN VPNIDKADIS VHCHNDLGLA VANSLSAILN GATQIEGTIN GLGERAGNAA
VEEIIMGLET RKDFYNVTHN FDTTQIYRTS KLVSSLTGVK VPPNKAIVGS NAFAHESGIH
QHGVLAEKTT YEIMTPESIG LSTNRMVLGK LSGRHAFEER LKELGYNNLT DEEIQKAFEM
FKDLADRKKT VTDKDIEALI GAKVSKVPEV YELESFQITS GNKSVATATI SLKKSEEIIT
EAATGDGPID AAFNAMERVV GMNFKLEDYF LESVTEGKDA LGEVTVKISK DDIAVLGRGI
STDVIEASIK SYLNAINKII SEEKLLGGK
//
