ID A0A0P7WJG6_9BACT Unreviewed; 401 AA.
AC A0A0P7WJG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN Name=leuA {ECO:0000313|EMBL:KPQ00460.1};
GN ORFNames=HLUCCA01_00940 {ECO:0000313|EMBL:KPQ00460.1};
OS Bacteroidetes bacterium HLUCCA01.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1666909 {ECO:0000313|EMBL:KPQ00460.1, ECO:0000313|Proteomes:UP000050310};
RN [1] {ECO:0000313|EMBL:KPQ00460.1, ECO:0000313|Proteomes:UP000050310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA01 {ECO:0000313|EMBL:KPQ00460.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396}.
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:KPQ00460.1}.
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DR EMBL; LIHN01000001; KPQ00460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WJG6; -.
DR STRING; 1666909.HLUCCA01_00940; -.
DR PATRIC; fig|1666909.3.peg.824; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000050310; 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-UniPathway.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
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 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 401 AA; 44114 MW; 7F2D0B7287D19864 CRC64;
MNSHIQIFDT TLRDGEQSPG FSMTHSEKMR MAEQLEQLGV DVIEAGFPIA SEGDFQAVKE
ISRQISNCQV AGLCRIKKDD ISRAWEALEH ARFPRIHTFV ATSDIHLVHK LNMSREQVLE
AAVEGVTYAR SLCDIVEFSA EDASRTDPDF LCEITRAVIQ AGATIVNIPD TVGFAVPEEF
GALIRKLKTE VPNIEQAVIS VHCHNDLGLA VANSLAAVQN GAGQIECTIN GIGERAGNAS
LEEIVMALAV RKSFYNTDTK LDTTQLYPAS QLLAEITGNH VQPNKAIVGR NAFAHEAGIH
QDGVLKNPLT YEIMTPQTVG VPQNSLVLGK HSGRRALADR MNKLGYTFTK DEIDKVYTCF
TVLADLKKNI TDQDLTYLAE RGLEMAGEQN MSQNLQEYIN Q
//
