ID   CIMA_SULAC              Reviewed;         523 AA.
AC   Q4J6H1;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000305|PubMed:31330039};
DE            EC=2.3.1.182 {ECO:0000269|PubMed:31330039};
DE   AltName: Full=Citramalate synthase {ECO:0000303|PubMed:31330039};
DE            Short=CMS {ECO:0000303|PubMed:31330039};
GN   Name=cimA {ECO:0000312|EMBL:AAY81610.1};
GN   OrderedLocusNames=Saci_2325 {ECO:0000312|EMBL:AAY81610.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=31330039; DOI=10.1002/1873-3468.13550;
RA   Suzuki T., Akiyama N., Yoshida A., Tomita T., Lassak K., Haurat M.F.,
RA   Okada T., Takahashi K., Albers S.V., Kuzuyama T., Nishiyama M.;
RT   "Biochemical characterization of archaeal homocitrate synthase from
RT   Sulfolobus acidocaldarius.";
RL   FEBS Lett. 594:126-134(2020).
CC   -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC       to form (R)-citramalate. Makes part of a pathway for isoleucine
CC       biosynthesis, i.e. the citramalate-dependent pathway. Also displays a
CC       low alpha-isopropylmalate synthase activity, using 2-oxoisovalerate as
CC       substrate, but is unable to use 2-oxoglutarate.
CC       {ECO:0000269|PubMed:31330039}.
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=2.3.1.182;
CC         Evidence={ECO:0000269|PubMed:31330039};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19046;
CC         Evidence={ECO:0000269|PubMed:31330039};
CC   -!- ACTIVITY REGULATION: Inhibited by isoleucine.
CC       {ECO:0000269|PubMed:31330039}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from pyruvate: step 1/3. {ECO:0000269|PubMed:31330039}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show slow growth in MM,
CC       and the addition of isoleucine or citramalate restores the growth of
CC       the mutant. {ECO:0000269|PubMed:31330039}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000077; AAY81610.1; -; Genomic_DNA.
DR   RefSeq; WP_011279112.1; NC_007181.1.
DR   AlphaFoldDB; Q4J6H1; -.
DR   SMR; Q4J6H1; -.
DR   STRING; 330779.Saci_2325; -.
DR   EnsemblBacteria; AAY81610; AAY81610; Saci_2325.
DR   GeneID; 3473572; -.
DR   KEGG; sai:Saci_2325; -.
DR   PATRIC; fig|330779.12.peg.2335; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_7_0_2; -.
DR   OMA; KSWDFHV; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.160.270; -; 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   PANTHER; PTHR43538; PTHR43538; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF08502; LeuA_dimer; 1.
DR   SMART; SM00917; LeuA_dimer; 1.
DR   SUPFAM; SSF110921; SSF110921; 1.
DR   TIGRFAMs; TIGR00977; citramal_synth; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Isoleucine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..523
FT                   /note="(R)-citramalate synthase"
FT                   /id="PRO_0000448053"
FT   DOMAIN          6..272
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   523 AA;  58128 MW;  87B8481E02E78E69 CRC64;
     MFTKSVEVLD TTLRDGAQTA NISFTLNDKI RIALLLDELG VDYIEGGWPS SNPKDEEFFK
     EIKKYKLTKA RIAAFGSTRK KESTAKEDQS LNSIIKADVD VGVLFGKSWS LHVTDVLKIS
     LEENLDIIYD SVNYLKSHGL RVVYDAEHFY QGYKENREYA LKAVKTAEEA GADVIVLCDT
     NGGTLPHEVY NITKDVVNHV KVKIGLHMHN DSGGAVANTV MGVVAGARHV QGTINGIGER
     TGNADLIQVI PNIMLKLGLN SLKGNESLKK LKEVSRVVYE IIGVHPNPYQ PYVGDFAFTH
     KAGVHADAVM KVTRAYEHID PTLVGNNRRF VISEVAGSSN VIYYLEKLGI KVDKKDPRVR
     NAVQRIKELE NRGYSFDLAP ASAVLVALRD LGMYRDLIKV EYWKVMNEKE LAIAIVKVNG
     QLEVAEGVGP VHSVDIALRK ALQKVYPQIN KVKLTDYRVI LPGEIKNTES VVRVTIEFTD
     GEKNWRTEGV STSVIEASVI ALIDGLDYYL QTEKLIKSEV INN