ID A0A0N8KQW9_9EURY Unreviewed; 449 AA.
AC A0A0N8KQW9;
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:KPQ43306.1};
DE EC=2.3.3.13 {ECO:0000313|EMBL:KPQ43306.1};
GN Name=leuA_2 {ECO:0000313|EMBL:KPQ43306.1};
GN ORFNames=MPEBLZ_02136 {ECO:0000313|EMBL:KPQ43306.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ43306.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ43306.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154}.
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:KPQ43306.1}.
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DR EMBL; LKCM01000160; KPQ43306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KQW9; -.
DR PATRIC; fig|1719120.3.peg.2336; -.
DR Proteomes; UP000050360; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KPQ43306.1};
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:0000313|EMBL:KPQ43306.1}.
FT DOMAIN 1..208
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 449 AA; 48317 MW; 4E7DCCCA0B84A6EE CRC64;
MSSEGEKASV RKIVDAGLNL KVCGLARVIK SDIDTCLDCG VDMVHTFVST SDVQRISTIK
KSRDEVYSMA IDAVEYIKDH GAKCMFSAMD ATRTDADYLI NIYKGVESAH CDIINVPDTV
GVIVPSAMYK LIGEIAKNVK IPIDVHCHND FGLAVANSLS AVEAGASQVQ VTVNGLGERA
GNADLAETVM GLHALYGAKT NIKTKYIVET SHLVERLTEV RMPPTMPIVG DNAFAHESGI
HTHGVLVRSD TFEPGVMTPE MVGHKRRIVL GKHAGKHAVK QSLEFAGLQP DDEQLNEIMK
RIKDIGDKGK RVTDADLYSI AESIMGNISK SEQAIVLKEV SVMTGNIITP TATVKAIVNG
QERLGAHIGV GPVDAALNTV TSILGEYKFK LRDFRIEAIS GGSDALAEVL IGVEDEKGRI
VSARATNEDI VMASVEALVA AINQLMRKR
//
