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Database: UniProt
Entry: A0A0M1P7H7_9BACL
LinkDB: A0A0M1P7H7_9BACL
Original site: A0A0M1P7H7_9BACL 
ID   A0A0M1P7H7_9BACL        Unreviewed;       538 AA.
AC   A0A0M1P7H7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=AM231_15770 {ECO:0000313|EMBL:KOR90438.1};
OS   Paenibacillus solani.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR90438.1, ECO:0000313|Proteomes:UP000036932};
RN   [1] {ECO:0000313|Proteomes:UP000036932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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}.
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:KOR90438.1}.
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DR   EMBL; LIUT01000001; KOR90438.1; -; Genomic_DNA.
DR   RefSeq; WP_053492142.1; NZ_LIUT01000001.1.
DR   AlphaFoldDB; A0A0M1P7H7; -.
DR   PATRIC; fig|1705565.3.peg.5235; -.
DR   OrthoDB; 9804858at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000036932; 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:UP000036932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          5..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   538 AA;  58408 MW;  5530E51D474269D1 CRC64;
     MSKSISIFDT TLRDGTQGEG ISLSADDKVK IAKKLNALGV HYIEGGIPGS NSKDIEFFKR
     VQDLGFTSKV VAFGSTRRKG GIADQDANLQ RILESGVSAA TLVGKSWDFH VHTALQTTLE
     ENLAMIHDSI AFLKRKGLEV MFDAEHFFDG FKNNPEYAVA VMSTARNAGA DWLVMCDTNG
     GSLPHEVASI VTSLTNQIPG APLGVHTHND CELAVANTLS AVQAGVRQVQ GTMNGYGERC
     GNANLCSIIP NLQLKLDYEC IGDDNLGTLT NTARYISEIA NVNMPVNQPY VGNAAFAHKG
     GIHVSAILRD SRTYEHIEPE KVGNKQRVLV SELAGQSNIV SKAQDMGLNF DPASEQSKHI
     IGKIKDLEHE GYQFEGADAS LELLLREANG ELKELFTFES FKMLVEKTAG QPVVSEAFVK
     VNVAGESIYT AAEGNGPVNA LDNALRKALV QYFPTLKEMH LADYKVRVLD DKDATAAKVR
     VLIESKNFEN SWNTVGVSSN VIEASWEALV DSMRYALLGQ ISPEQVHQSA ARQGLVNH
//
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