ID A0A1V9FE72_9BACT Unreviewed; 507 AA.
AC A0A1V9FE72;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:OQP56587.1};
GN ORFNames=A4R26_05355 {ECO:0000313|EMBL:OQP56587.1};
OS Niastella populi.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP56587.1, ECO:0000313|Proteomes:UP000192276};
RN [1] {ECO:0000313|Proteomes:UP000192276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA Chen L., Zhuang W., Wang G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:OQP56587.1}.
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DR EMBL; LWBP01000199; OQP56587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9FE72; -.
DR STRING; 550983.A4R26_05355; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000192276; Unassembled WGS sequence.
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:UP000192276};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 8..270
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 507 AA; 56635 MW; 43080BB96311EF27 CRC64;
MPGDQRHIEI MDTTLRDGEQ TSGVSFSPTE KLTIAQLLLT EVKVNRIEIA SARVSEGEFE
AVKAITKWAK SNGFLNQVEV LTFVDGDVSI QWMQQAGAKV MNLLTKGSLN HLTHQLKKKP
EQHFAEIADV IKLARKKGIE VNVYLEDWSN GMRHSKEYVF QYLDFIQKMP VKRIMLPDTL
GILTPAEVTE YISAIVQRYP GLHFDFHAHN DYDLGTANVL EGVKAGAHGI HLTINGMGER
AGNAPLASAI AVMNDFVPEV KTSVVEASLY RVSKLVETFS GFRIPVNKPV VGENVFTQTA
GIHADGDKKN KLYFSDLMPE RFGRTRRYAL GKTSGKANIE NNLAQLGIQL SEPDLKKVTQ
RIIELGDKKE VVTQADLPYI ISDVIDSRNI TEKVRIENYV LTHSKNLRPS VTVEISINGE
LYEEHSQGDG QYDAFVNALK KVYKRMKKEL PILTDYAVRI PPGGKSDALC ETVITWSYNG
KEFKTRGLDS DQTVSAIKAT QKMLNLI
//
