ID A0A0N1MRM8_9SPHN Unreviewed; 557 AA.
AC A0A0N1MRM8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572};
GN Name=leuA {ECO:0000256|HAMAP-Rule:MF_00572};
GN ORFNames=ADT71_26115 {ECO:0000313|EMBL:KPH58774.1}, EDF59_102256
GN {ECO:0000313|EMBL:TCM42292.1};
OS Novosphingobium sp. ST904.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH58774.1, ECO:0000313|Proteomes:UP000037878};
RN [1] {ECO:0000313|EMBL:KPH58774.1, ECO:0000313|Proteomes:UP000037878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:KPH58774.1,
RC ECO:0000313|Proteomes:UP000037878};
RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA Vangronsveld J.;
RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT stimulates plant growth.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TCM42292.1, ECO:0000313|Proteomes:UP000295740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:TCM42292.1,
RC ECO:0000313|Proteomes:UP000295740};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (MAR-2019) 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-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000256|HAMAP-
CC Rule:MF_00572}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00572};
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_00572}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767,
CC ECO:0000256|HAMAP-Rule:MF_00572}.
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:KPH58774.1}.
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DR EMBL; LGJH01000164; KPH58774.1; -; Genomic_DNA.
DR EMBL; SLVC01000002; TCM42292.1; -; Genomic_DNA.
DR RefSeq; WP_054441689.1; NZ_SLVC01000002.1.
DR AlphaFoldDB; A0A0N1MRM8; -.
DR STRING; 1684385.ADT71_26115; -.
DR PATRIC; fig|1684385.3.peg.3520; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000037878; Unassembled WGS sequence.
DR Proteomes; UP000295740; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00970; leuA_yeast; 1.
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 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_00572};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572};
KW Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00572};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00572}; Reference proteome {ECO:0000313|Proteomes:UP000037878};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00572}.
FT DOMAIN 33..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 441..557
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ SEQUENCE 557 AA; 61486 MW; 7AA6B6F3755C643F CRC64;
MTMLQDPSVK YRPFPQIDLP NRQWPSQVIT KAPRWLSTDL RDGNQALIDP MGAEKKNRFF
DLLVKVGLKE IEVGFPSAGA TEFDFINGLV KNDRIPEDVL VQVLTQSRED LITRSFESLE
GVHAAIVHLY NAVSPLWRNV VFGMDKQEIK GIAQGGARIL RDQAAKYPAT KWQFEYSPET
FSTAELDFSI EVCEAVMEIL QPTPENPIIL NLPATVEAAT PNVYADQIEY FCRNLPNRES
AVISLHTHND RGTGVAAAEL GLMAGADRVE GCLFGNGERT GNCCLVTVAM NMYTQGVNPE
LDFSDIDEVI QTVEYCNQLK VGERHPYGGE LVFTAFSGSH QDAIKKGFAA QEKRNDQIWS
VPYLPIDPAD LGRDYEAVIR VNSQSGKGGF AWVIEQDQGL KLPKRMQAHF SKHVQELADE
LGRELQASDI WEVFRKAYRI DDPQHFQLID WEEAKAADGT RVFAGKIGVD GKEQSVSGRG
NGLISSVTAT LAESFGVTLD VRDYAEHSMG KSSDARAAAY VECVAPDGRV IWGVGIDEDV
ATASVRAVLS AANTARI
//
