ID A0A1I4ET11_9FIRM Unreviewed; 523 AA.
AC A0A1I4ET11;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=SAMN02983006_00137 {ECO:0000313|EMBL:SFL08852.1};
OS Halanaerobium salsuginis.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL08852.1, ECO:0000313|Proteomes:UP000199006};
RN [1] {ECO:0000313|EMBL:SFL08852.1, ECO:0000313|Proteomes:UP000199006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL08852.1,
RC ECO:0000313|Proteomes:UP000199006};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00034270};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; FOTI01000001; SFL08852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ET11; -.
DR STRING; 29563.SAMN02983006_00137; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000199006; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07941; DRE_TIM_LeuA3; 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; IPR005675; Citramal_synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00977; citramal_synth; 1.
DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/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; 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 Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Reference proteome {ECO:0000313|Proteomes:UP000199006};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 3..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 523 AA; 57980 MW; AAEE7EDFF87B3421 CRC64;
MGLALYDTTL RDGSQGEGIS LSLDDKLRIT KQLDKFGIDF IEGGWPGSNP KDEAYFAAVK
NLELKQANVT AFSSTRRPNL KVSADNNILK LVEAGVDYVT IFAKSWDLHV REALQISLTE
NLAMIADTIE FLTEKGLHVF FDAEHFFDGY LANAEYAIKT IQTAADAGAE VLTLCDTNGG
MLPSRLRKII KTVKSEVTAP LGIHAHNDGN LAVANSLTAF EEGAVQIQGT VGGLGERCGN
ADLCSVIPTI QLKYETRLLS DKQLKQLKPL YFFVTETANL IPDNNKPYVG KSAFTHKGGI
HVSAVRKNPH TYEHIQPELV GNERRVLVSE LAGKSNLRYK LQELGFNLAD FSDGMIKKLI
KRVKSLESKG YQFEGAEASL ILLAFREFKG YQSFFEIEDF RTNSINRNNQ TYSEAVVKMT
VKGKKVHIAA EGDGPVNALD NCFRKALMNF YPEIAKTKLI DYKVRVLNGN DGTAAKVRVL
IESSDFEKSW TTVGVSTNII QASWDALIDS IEYWLLIEES III
//
