ID   CIRSY_DEHMC             Reviewed;         415 AA.
AC   P0DO96;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Citrate (Re)-synthase {ECO:0000303|PubMed:21784924};
DE            EC=2.3.3.3 {ECO:0000269|PubMed:21784924};
DE   AltName: Full=Re face-specific citrate synthase {ECO:0000303|PubMed:21784924};
DE   AltName: Full=Re-citrate synthase {ECO:0000303|PubMed:21784924};
GN   OrderedLocusNames=cbdbA1708;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=CBDB1;
RX   PubMed=21784924; DOI=10.1128/jb.05120-11;
RA   Marco-Urrea E., Paul S., Khodaverdi V., Seifert J., von Bergen M.,
RA   Kretzschmar U., Adrian L.;
RT   "Identification and characterization of a re-citrate synthase in
RT   Dehalococcoides strain CBDB1.";
RL   J. Bacteriol. 193:5171-5178(2011).
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl
CC       coenzyme A (acetyl-CoA) with oxaloacetate to form citrate. This enzyme
CC       is highly Re-face stereospecific with respect to the C-2 of
CC       oxaloacetate. {ECO:0000269|PubMed:21784924}.
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:21784924};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:21784924};
CC   -!- ACTIVITY REGULATION: Inhibited by citrate and under aerobic conditions.
CC       {ECO:0000269|PubMed:21784924}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 uM for oxaloacetate {ECO:0000269|PubMed:21784924};
CC         KM=75 uM for acetyl-CoA {ECO:0000269|PubMed:21784924};
CC         Vmax=9.1 umol/sec/mg enzyme toward acetyl-CoA
CC         {ECO:0000269|PubMed:21784924};
CC         Vmax=11.2 umol/sec/mg enzyme toward oxaloacetate
CC         {ECO:0000269|PubMed:21784924};
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ965256; CAI83711.1; -; Genomic_DNA.
DR   RefSeq; WP_011310049.1; NC_007356.1.
DR   AlphaFoldDB; P0DO96; -.
DR   SMR; P0DO96; -.
DR   KEGG; deh:cbdbA1708; -.
DR   HOGENOM; CLU_022158_4_2_0; -.
DR   OMA; SNMFAHE; -.
DR   BRENDA; 2.3.3.3; 12662.
DR   SABIO-RK; P0DO96; -.
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   Pfam; PF00682; HMGL-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Magnesium; Manganese; Transferase.
FT   CHAIN           1..415
FT                   /note="Citrate (Re)-synthase"
FT                   /id="PRO_0000436431"
FT   DOMAIN          4..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   415 AA;  45619 MW;  443E2F2408F22DA8 CRC64;
     MGKIFIIDVT NRDGVQTARL GLSKLEKTLI NIYLDEMGIF QSEFGFPTTK HERGYVEANL
     ELAKMGVIKN LRLEGWIRAI VADVDLAFRR APSLKHLNLS ISTSEQMING KFQGRKVFKD
     IIEDMTIAVN AAYAKGAETV GVNAEDASRT SIVNLIEFGK AAKEVGATRL RYCDTLGYDN
     PFTIYETART LAEKVGMPIE IHCHGDLGMA IGNSLAGAKG VIDGGQDVYV NTTVNGIGER
     AGNADLVAFL LAILKSKGFG EKYQLGHEVD LSKAWKIARF ASYAFDVEIP INQPGVGRNC
     FAHASGIHAD GVIKDSQNYE LYGYEELGRG EALMVETGRE ICAGQYSGIS GFRHVMGNMS
     VELPEDKDEA NKILELVRYA NVEAHKPLVE DELIFIAKYP EISRRLLTLT PLMND