ID   CITEL_MYCTO             Reviewed;         273 AA.
AC   P9WPE0; L0TCQ1; O06162; Q7D713;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Citrate lyase subunit beta-like protein;
DE            EC=4.1.-.-;
GN   Name=citE; OrderedLocusNames=MT2573;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May play a role in fatty acid biosynthesis. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate lyase
CC       beta subunit-like subfamily. {ECO:0000305}.
CC   -!- CAUTION: This organism lacks the other subunits that are necessary for
CC       ATP-independent citrate lyase activity. Even though this protein has
CC       clear similarity to citrate lyase beta subunit, it is expected to have
CC       a somewhat different enzyme activity. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46877.1; -; Genomic_DNA.
DR   PIR; B70550; B70550.
DR   RefSeq; WP_003412766.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPE0; -.
DR   SMR; P9WPE0; -.
DR   EnsemblBacteria; AAK46877; AAK46877; MT2573.
DR   GeneID; 45426492; -.
DR   KEGG; mtc:MT2573; -.
DR   PATRIC; fig|83331.31.peg.2775; -.
DR   HOGENOM; CLU_044864_2_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..273
FT                   /note="Citrate lyase subunit beta-like protein"
FT                   /id="PRO_0000426968"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   273 AA;  28886 MW;  5FD8634672FF5C7C CRC64;
     MNLRAAGPGW LFCPADRPER FAKAAAAADV VILDLEDGVA EAQKPAARNA LRDTPLDPER
     TVVRINAGGT ADQARDLEAL AGTAYTTVML PKAESAAQVI ELAPRDVIAL VETARGAVCA
     AEIAAADPTV GMMWGAEDLI ATLGGSSSRR ADGAYRDVAR HVRSTILLAA SAFGRLALDA
     VHLDILDVEG LQEEARDAAA VGFDVTVCIH PSQIPVVRKA YRPSHEKLAW ARRVLAASRS
     ERGAFAFEGQ MVDSPVLTHA ETMLRRAGEA TSE