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Database: UniProt
Entry: A0A101TPX1_9ACTN
LinkDB: A0A101TPX1_9ACTN
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ID   A0A101TPX1_9ACTN        Unreviewed;       534 AA.
AC   A0A101TPX1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=AQJ67_34225 {ECO:0000313|EMBL:KUN96290.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUN96290.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUN96290.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUN96290.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
RL   Submitted (OCT-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:KUN96290.1}.
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DR   EMBL; LMWY01000044; KUN96290.1; -; Genomic_DNA.
DR   RefSeq; WP_062723233.1; NZ_KQ948936.1.
DR   AlphaFoldDB; A0A101TPX1; -.
DR   STRING; 661399.AQJ67_34225; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000053429; 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   Reference proteome {ECO:0000313|Proteomes:UP000053429};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          11..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   534 AA;  57701 MW;  56086CC096F3EA9E CRC64;
     MTATSELDDS FHVFDTTLRD GAQREGINLT VADKLAIARH LDEFGVGFIE GGWPGANPRD
     TEFFARAQQE IDFRHAQLVA FGSTRRAGAK ASEDPQVKAL LESGAPVITL VAKSHDRHVE
     LALRTTLDEN LAMIQDTVAY LCSQGRRVFV DCEHFFDGYR ANPEYAKSVV RTASQAGADV
     VILCDTNGGM LPAQVQAVVA TVLVDTGARL GIHAQDDTGC AVANTLAAVD AGATHVQCTA
     NGYGERVGNA NLFPVVAALE LKYGKKVLPD GRLREMTRIS HAIAEVVNLT PSTHQPYVGV
     SAFAHKAGLH ASAIKVDPDL YQHIDPERVG NTMRMLVSDM AGRASIELKG KELGIDLGGD
     RELVGRVVER VKERELKGYT YEAADASFEL LLRAEVEGKP LKYFDVESWR AIVEDRPDGT
     HANEATVKLF AKGERIVATA EGNGPVNALD RALRVALEKI YPQLAQLDLV DYKVRILEGV
     HGTQSTTRVL ISTSDGSGEW STVGVAENVI AASWQALEDA YTYGLLRAGV EPAE
//
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