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Database: UniProt
Entry: W7YVT8_9BACL
LinkDB: W7YVT8_9BACL
Original site: W7YVT8_9BACL 
ID   W7YVT8_9BACL            Unreviewed;       539 AA.
AC   W7YVT8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=JCM16418_456 {ECO:0000313|EMBL:GAF06499.1};
OS   Paenibacillus pini JCM 16418.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF06499.1, ECO:0000313|Proteomes:UP000019364};
RN   [1] {ECO:0000313|EMBL:GAF06499.1, ECO:0000313|Proteomes:UP000019364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF06499.1,
RC   ECO:0000313|Proteomes:UP000019364};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT   Rhizosphere of Pine Tree.";
RL   Genome Announc. 2:e00210-14(2014).
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:GAF06499.1}.
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DR   EMBL; BAVZ01000001; GAF06499.1; -; Genomic_DNA.
DR   RefSeq; WP_036645593.1; NZ_BAZT01000001.1.
DR   AlphaFoldDB; W7YVT8; -.
DR   STRING; 1236976.JCM16418_456; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9804858at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000019364; 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; 3.30.160.270; -; 1.
DR   Gene3D; 4.10.430.20; -; 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:UP000019364};
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   539 AA;  59111 MW;  CB4B4F357B7BC6EE CRC64;
     MSKSISIFDT TLRDGTQGEG ISLSADDKLK IAKKLDDLGV QYIEGGIPGS NTKDIEFFKR
     VQELGLNAKI TAFGSTRRKG TVASQDANLQ RILESGCQAA TLVGKAWDFH VHTALQTTLE
     ENLAMIYDSI AYLKQQGQEV IFDAEHFFDG YKNNTEYAIS VVRKAQEAGA DWITMCDTNG
     GTLPHEVHEI VSSLTSMIPQ AHFSIHTHND CELAVANTLS AVQAGARQVQ GTINGYGERC
     GNANLCSIIP SLELKMGYQT IGTDKLMQLT STARFVSEIA NVNMPVNQPY VGNAAFAHKG
     GIHVSAILRD SRTYEHIVPE LVGNKQRVLV SELAGQSNIV SKAKDMGLEL DSTSEHSRKV
     IDKIKDLEHQ GYQFEAADAS LELLLREANG EMKELFSFES FKMLVEKTAG RAVVSEAFVK
     LNVAGNMVYT AAEGNGPVNA LDNALRKALV QYFPDLKEMH LSDYKVRVLD EKDATAAKVR
     VLIESRNISN SWNTVGVSEN VIEASWEALV DSMRYALMGK IMQGNEEGED TTHRGLVNH
//
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