ID   CIRSY_SYNAS             Reviewed;         629 AA.
AC   Q2LTE1;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Citrate (Re)-synthase {ECO:0000305};
DE            EC=2.3.3.3 {ECO:0000269|PubMed:23378508};
DE   AltName: Full=Re-citrate synthase {ECO:0000303|PubMed:23378508};
GN   ORFNames=SYN_02536 {ECO:0000312|EMBL:ABC77353.2};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX   PubMed=23378508; DOI=10.1128/jb.02185-12;
RA   Kim M., Le H., McInerney M.J., Buckel W.;
RT   "Identification and characterization of re-citrate synthase in Syntrophus
RT   aciditrophicus.";
RL   J. Bacteriol. 195:1689-1696(2013).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with oxaloacetate to form citrate. {ECO:0000269|PubMed:23378508}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC         Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.3;
CC         Evidence={ECO:0000269|PubMed:23378508};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16846;
CC         Evidence={ECO:0000269|PubMed:23378508};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:23378508};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:23378508};
CC   -!- ACTIVITY REGULATION: Inhibited by p-hydroxymercuribenzoate and EDTA.
CC       {ECO:0000269|PubMed:23378508}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=130 uM for acetyl-CoA {ECO:0000269|PubMed:23378508};
CC         KM=85 uM for oxaloacetate {ECO:0000269|PubMed:23378508};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23378508}.
CC   -!- INDUCTION: Expressed under all growth conditions.
CC       {ECO:0000269|PubMed:23378508}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000252; ABC77353.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LTE1; -.
DR   SMR; Q2LTE1; -.
DR   STRING; 56780.SYN_02536; -.
DR   EnsemblBacteria; ABC77353; ABC77353; SYN_02536.
DR   KEGG; sat:SYN_02536; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_5_0_7; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0036440; F:citrate synthase activity; IEA:RHEA.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Manganese; Reference proteome; Transferase.
FT   CHAIN           1..629
FT                   /note="Citrate (Re)-synthase"
FT                   /id="PRO_0000449458"
FT   DOMAIN          59..329
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          497..601
FT                   /note="Cache"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   629 AA;  71767 MW;  A4E404229F970D83 CRC64;
     MAKWNPQKRV LNHEHTRFWR FELRDVDEPN LQKEVFPYDE VSRIDFDHRI IPIQPAEEIF
     ITDTTFRDGQ QARPPYTTQQ IVDLYQMMSR LGGYNGIIRQ TEFFLYSNRD KEAVRMCQDL
     GLQYPEITGW IRAAREDIPL VKEAGLKETG ILTSVSDYHI FLKLNMTRSQ ALEEYLGIVK
     AILDAGIVPR CHFEDITRAD IYGFCIPFAI ELMKLREESG VDIKIRLCDT MGYGVTYPGA
     SLPRGVDKLV RAFIDDADVP GRLLEWHGHN DFHKALINAT TAWLYGCSAA NSTLLGLGER
     TGNPPIEGLI IEYIGLMGKT NGIDTTVITD IANYFKNEIE YKIPSNYPFV GADFNVTRAG
     VHADGLIKSE EIYNIFNTTK ILKRPIVPMI TDKSGKAGIA YWINSHFGLS GDSTVDKRHP
     GISKINKWIA DEYELGRVTT ISTEELEAKV RKYMPELFMS DLERIKFKAA EAAIAVLRKI
     IDDPAMKTMQ PELQEPVMQR FIEEYPSIQF AYVVDMNGKK TTRNITNIVD RAKYENYGVG
     TDQSDREWFI KPLQTGKLHV TDFYISKMTG ALCFTVSEPI TDDNDDMVGI FGVDIRVEDL
     VKEPEYIAEA TQIALKAEYD AKYKSDHWL