ID A0A0N8PWE8_9ARCH Unreviewed; 507 AA.
AC A0A0N8PWE8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:KPV63725.1};
GN Name=leuA_2 {ECO:0000313|EMBL:KPV63725.1};
GN ORFNames=AOA66_0681 {ECO:0000313|EMBL:KPV63725.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63725.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV63725.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63725.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, 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:KPV63725.1}.
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DR EMBL; LIHK01000017; KPV63725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PWE8; -.
DR STRING; 1700836.AOA66_0681; -.
DR KEGG; barb:AOA66_0681; -.
DR PATRIC; fig|1700836.3.peg.214; -.
DR Proteomes; UP000050284; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
DR PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; HOMOCITRATE 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 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:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 9..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 507 AA; 54586 MW; E34F4C39D2115FE2 CRC64;
MKSKNVKYVS IFDTTLRDGE QTPGVSLTTE EKLEIARQLD RLGVDVIEAG TPISSEGEKR
AVREITKAGL NAEICALART TRVDVDAAIA CDVGSVHTFI STSDVQMKHA VNMTPEQVLS
ATIDSVEYIK DHGLICEFSP MDATRTEINF LKRVCKAAEE AGADRINIPD TVGIMTPVTM
RKLIEDVKSV VGVPISVHCH NDFGMAVANS LAGVEAGASQ IHVTVNGLGE RAGNAALEEV
VMALHLIYNR KTGINTKLLY DTSRLVAKLT GVMIQPNKAI VGENAFAHES GIHTRGVTVV
PLTFEPIKPE LVGRKRKLVA GKLSGTSGIK AELKEAGIYP NKDQLGEIVR RVKELGDKGK
TVTDADLLAI TRSVMGKVVK EKRIVDLTDL AVVTGIRVIP TASVRLVLDG KEYVTSETGL
GPVDAAIKAV QKLTADLAEV RLKEYRIEAT TGGSDAMGEV IIKVEDRDGN VVSARATHED
IVMASVEAMI NAINKSLLKR RNRDKQA
//
