ID   CITEL_MYCTU             Reviewed;         273 AA.
AC   P9WPE1; 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=Rv2498c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP   MAGNESIUM IONS, AND SUBUNIT.
RX   PubMed=17064730; DOI=10.1016/j.jmb.2006.09.086;
RA   Goulding C.W., Bowers P.M., Segelke B., Lekin T., Kim C.Y.,
RA   Terwilliger T.C., Eisenberg D.;
RT   "The structure and computational analysis of Mycobacterium tuberculosis
RT   protein CitE suggest a novel enzymatic function.";
RL   J. Mol. Biol. 365:275-283(2007).
CC   -!- FUNCTION: May play a role in fatty acid biosynthesis. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17064730}.
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; AL123456; CCP45292.1; -; Genomic_DNA.
DR   PIR; B70550; B70550.
DR   RefSeq; NP_217014.1; NC_000962.3.
DR   RefSeq; WP_003412766.1; NZ_NVQJ01000063.1.
DR   PDB; 1U5H; X-ray; 1.65 A; A=1-273.
DR   PDB; 1U5V; X-ray; 1.85 A; A=1-273.
DR   PDB; 1Z6K; X-ray; 2.30 A; A=1-273.
DR   PDB; 6AQ4; X-ray; 1.82 A; A/B/C=1-273.
DR   PDBsum; 1U5H; -.
DR   PDBsum; 1U5V; -.
DR   PDBsum; 1Z6K; -.
DR   PDBsum; 6AQ4; -.
DR   AlphaFoldDB; P9WPE1; -.
DR   SMR; P9WPE1; -.
DR   STRING; 83332.Rv2498c; -.
DR   DrugBank; DB01942; Formic acid.
DR   PaxDb; P9WPE1; -.
DR   DNASU; 887466; -.
DR   GeneID; 45426492; -.
DR   GeneID; 887466; -.
DR   KEGG; mtu:Rv2498c; -.
DR   TubercuList; Rv2498c; -.
DR   eggNOG; COG2301; Bacteria.
DR   OMA; AWLFCPA; -.
DR   PhylomeDB; P9WPE1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IPI:MTBBASE.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IPI:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..273
FT                   /note="Citrate lyase subunit beta-like protein"
FT                   /id="PRO_0000286388"
FT   BINDING         64
FT                   /ligand="substrate"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         112
FT                   /ligand="substrate"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   TURN            3..5
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          8..14
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           21..27
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           71..81
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           96..100
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   TURN            101..104
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           114..118
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           120..125
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           157..172
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           188..201
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   STRAND          204..210
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           214..220
FT                   /evidence="ECO:0007829|PDB:1U5H"
FT   HELIX           225..239
FT                   /evidence="ECO:0007829|PDB:6AQ4"
FT   STRAND          243..247
FT                   /evidence="ECO:0007829|PDB:6AQ4"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:6AQ4"
FT   HELIX           254..265
FT                   /evidence="ECO:0007829|PDB:6AQ4"
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