ID   CIRSY_CLOK5             Reviewed;         453 AA.
AC   A5N6T4;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Citrate (Re)-synthase {ECO:0000305};
DE            EC=2.3.3.3 {ECO:0000269|PubMed:17400742};
DE   AltName: Full=Re-citrate synthase {ECO:0000303|PubMed:17400742};
GN   OrderedLocusNames=CKL_0973 {ECO:0000312|EMBL:EDK33015.1};
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=17400742; DOI=10.1128/jb.00198-07;
RA   Li F., Hagemeier C.H., Seedorf H., Gottschalk G., Thauer R.K.;
RT   "Re-citrate synthase from Clostridium kluyveri is phylogenetically related
RT   to homocitrate synthase and isopropylmalate synthase rather than to Si-
RT   citrate synthase.";
RL   J. Bacteriol. 189:4299-4304(2007).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with oxaloacetate to form citrate. This enzyme is highly Re-face
CC       stereospecific with respect to the C-2 of oxaloacetate.
CC       {ECO:0000269|PubMed:17400742}.
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:17400742};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:17400742};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:17400742};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17400742};
CC       Note=Can also use magnesium with lower efficiency.
CC       {ECO:0000269|PubMed:17400742};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate (pCMB), EDTA,
CC       Zn(2+) ions, and under aerobic conditions.
CC       {ECO:0000269|PubMed:17400742}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for oxaloacetate {ECO:0000269|PubMed:17400742};
CC         KM=50 uM for acetyl-CoA {ECO:0000269|PubMed:17400742};
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000673; EDK33015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5N6T4; -.
DR   SMR; A5N6T4; -.
DR   STRING; 431943.CKL_0973; -.
DR   EnsemblBacteria; EDK33015; EDK33015; CKL_0973.
DR   KEGG; ckl:CKL_0973; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_5_0_9; -.
DR   OMA; FEKELDY; -.
DR   SABIO-RK; A5N6T4; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0050450; F:citrate (Re)-synthase activity; IDA:UniProtKB.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Magnesium; Manganese; Reference proteome; Transferase.
FT   CHAIN           1..453
FT                   /note="Citrate (Re)-synthase"
FT                   /id="PRO_0000436430"
FT   DOMAIN          46..316
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   453 AA;  52135 MW;  06AED31931063CA2 CRC64;
     MKKCSYDYKL NNVNDPNFYK DIFPYEEVPK IVFNNIQLPM DLPDNIYITD TTFRDGQQSM
     PPYTSREIVR IFDYLHELDN NSGIIKQTEF FLYTKKDRKA AEVCMERGYE FPEVTSWIRA
     DKEDLKLVKD MGIKETGMLM SCSDYHIFKK LKMTRKETMD MYLDLAREAL NNGIRPRCHL
     EDITRADFYG FVVPFVNELM KMSKEANIPI KIRACDTLGL GVPYNGVEIP RSVQGIIHGL
     RNICEVPSES IEWHGHNDFY GVVTNSSTAW LYGASSINTS FLGIGERTGN CPLEAMIFEY
     AQIKGNTKNM KLHVITELAQ YFEKEIKYSV PVRTPFVGTD FNVTRAGIHA DGILKDEEIY
     NIFDTDKILG RPVVVAVSQY SGRAGIAAWV NTYYRLKDED KVNKNDSRID QIKMWVDEQY
     RAGRTSVIGN NELELLVSKV MPEVIEKTEE RAS