ID A0A0S8FXX2_9BACT Unreviewed; 530 AA.
AC A0A0S8FXX2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=AMK73_04360 {ECO:0000313|EMBL:KPK64970.1};
OS Planctomycetes bacterium SM23_32.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704029 {ECO:0000313|EMBL:KPK64970.1, ECO:0000313|Proteomes:UP000052164};
RN [1] {ECO:0000313|EMBL:KPK64970.1, ECO:0000313|Proteomes:UP000052164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_32 {ECO:0000313|EMBL:KPK64970.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK64970.1}.
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DR EMBL; LJUE01000063; KPK64970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FXX2; -.
DR PATRIC; fig|1704029.3.peg.617; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000052164; 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:InterPro.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 6..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 530 AA; 57694 MW; 983003C889D5C336 CRC64;
MSERPIRMYD TTLRDGCQAE GVALTVEDKL DVARRLDELG IHYIEGGYPL SNPKDQEFFR
RVGGLGLKSA RVAAFGSTRR ADTPVEQDKG LAAVLAAETP VVTIVAKAWD YHVANVIRAS
REENLRMVED SVRHLKAAGR EVIFDAEHFF DGCRTNADYA LQVARVAAEA GADCVVLCDT
NGGALTDEVG RVTALVVDAL PCPVGIRCHN DAGLAVANSI AAVQNGAVHV QGTMNGLGER
AGNADLCAVM ANINLKTPFC CATDEQLRKL TEISRFTCEV MNMIPDPRQP FVGASAFAHK
GGLHVDAMRK AEGAYEHVDP ALVGNERRFL LSELSGRASI LAKVEKYNIT RDREMVQELL
KKLLEMENEG YQFEAAEASF ELMAKRITGP FRRHFDVKSY HVSVIRHADG SLVTDGTVKL
DVGGRLMHTA SEGDGPVNAL DGALRKALEE HYPALKDMHL TDYKVRVINP KAATAARVRV
VIQSADSHRV WGTVGVSENI IDASWEALID SVEYKLLMED QAAAKGEEGA
//