ID A0A411ED94_9FLAO Unreviewed; 497 AA.
AC A0A411ED94;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:QBA65602.1};
GN ORFNames=EQY75_05780 {ECO:0000313|EMBL:QBA65602.1};
OS Muriicola soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Muriicola.
OX NCBI_TaxID=2507538 {ECO:0000313|EMBL:QBA65602.1, ECO:0000313|Proteomes:UP000290889};
RN [1] {ECO:0000313|EMBL:QBA65602.1, ECO:0000313|Proteomes:UP000290889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY002 {ECO:0000313|EMBL:QBA65602.1,
RC ECO:0000313|Proteomes:UP000290889};
RA Kang H.J., Kim S.B.;
RT "Muriicola soli sp. nov., isolated from soil.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP035544; QBA65602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411ED94; -.
DR KEGG; mur:EQY75_05780; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000290889; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.340; -; 1.
DR Gene3D; 3.30.160.740; -; 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; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF57; (R)-CITRAMALATE SYNTHASE CIMA; 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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000290889};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 1..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 497 AA; 55317 MW; 2608BB4A53CC7EFA CRC64;
MDTTLRDGEQ TSGVSFSASE KLTMAKLLLE ELRVDRIEIA SARVSEGEFQ SVKNILEWAS
ERGFEERVEV LTFVDGGLSL EWMQKSGAKV QNLLTKGSLN HLTHQLKKKP EEHFKEIAEV
IEQAGAMGIT TNVYLEDWSN GMRNSPDYVF NFLDFLATQP LKRVLLPDTL GVLTPNETGN
FISQIVKRYP EIHFDFHGHN DYDLSVANVM EAVKAGCHGL HLTVNGMGER AGNAPLASVV
AVLNDFLPEF RINVQESSLF KVSKLVSAFT GFVIPANKPI VGDNVFTQTA GIHADGDNKK
NLYFNDLLPE RFGRKRKYAL GKTSGKANIQ KNLQELGLTL NDEEIKKVTA RIIELGDKKE
RVTKDDLPYI ISDVLDSEGY QQKVFVKSYV LTHAKGLKPS TTVCVEFEGE SIEENAQGDG
QFDAFMNALR KVYRSKKKSL PNLVDYAVRI PPGSNSDALC ETVITWQDGD KEFATRGLDS
DQTVSAIKAT EKMLNII
//