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Database: UniProt
Entry: A0A0L8LQT7_9ACTN
LinkDB: A0A0L8LQT7_9ACTN
Original site: A0A0L8LQT7_9ACTN 
ID   A0A0L8LQT7_9ACTN        Unreviewed;       546 AA.
AC   A0A0L8LQT7;
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=ADK74_24305 {ECO:0000313|EMBL:KOG40516.1};
OS   Streptomyces decoyicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG40516.1, ECO:0000313|Proteomes:UP000037606};
RN   [1] {ECO:0000313|Proteomes:UP000037606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-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:KOG40516.1}.
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DR   EMBL; LGUU01000245; KOG40516.1; -; Genomic_DNA.
DR   RefSeq; WP_030084172.1; NZ_LGUU01000245.1.
DR   AlphaFoldDB; A0A0L8LQT7; -.
DR   PATRIC; fig|249567.6.peg.5395; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000037606; 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          19..282
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   546 AA;  59086 MW;  A3DA3DE1264C07C5 CRC64;
     MTDAQEPAPR PVGAVSDDFH VFDTTLRDGA QREGINLTVA DKLTIARHLD EFGVGFIEGG
     WPGANPRDTE FFQRAREEID FRHAQLVAFG ATRKAGVRVE DDQQVAALLE SRAPVITLVA
     KSHVGHVELA LRTTPEENLA MVRDTVAYLR AQGRRVFLDC EHFFDGYALD PVYAKQVVRT
     ASEAGADVVV LCDTNGGMLP AQVTAVVRTV VADTGARLGI HAQDDTGCAV ANTLAAVDAG
     ATHVQCTANG YGERVGNSNL FPVVAALELK YGRPVLPEGK LAETTRISHA IAEVVNLTPS
     THQPYVGVSA FAHKAGLHAS AIKVDPDLYQ HIDPALVGNT MRMLVSDMAG RASIELKGKE
     LGIDLSDDRE LVGRVVERVK ERELAGYTYE AADASFELLL REELQRAEGG RPRSYFRVES
     WRAIVEDRPD GTHANEATVK LWAKGERIVA TAEGNGPVNA LDRALRVGLE RIYPQLAHME
     LVDYKVRILE GALGTGSITR VLVSTSDGRG EWSTVGVAEN VIAASWQALD DAYAYGLLRA
     GVEPQE
//
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