CITEL_DEIRA
ID CITEL_DEIRA Reviewed; 284 AA.
AC Q9RUZ0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Citrate lyase subunit beta-like protein;
DE EC=4.1.-.-;
GN OrderedLocusNames=DR_1240;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP SUBSTRATE ANALOG, SUBUNIT, AND COFACTOR.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of citrate lyase beta subunit.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in fatty acid biosynthesis. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|Ref.2}.
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; AE000513; AAF10813.1; -; Genomic_DNA.
DR PIR; F75418; F75418.
DR RefSeq; NP_294964.1; NC_001263.1.
DR RefSeq; WP_010887883.1; NZ_CP015081.1.
DR PDB; 1SGJ; X-ray; 1.84 A; A/B/C=1-284.
DR PDBsum; 1SGJ; -.
DR AlphaFoldDB; Q9RUZ0; -.
DR SMR; Q9RUZ0; -.
DR STRING; 243230.DR_1240; -.
DR DrugBank; DB02637; Oxaloacetate Ion.
DR EnsemblBacteria; AAF10813; AAF10813; DR_1240.
DR KEGG; dra:DR_1240; -.
DR PATRIC; fig|243230.17.peg.1435; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_2_0; -.
DR InParanoid; Q9RUZ0; -.
DR OMA; WAMMETP; -.
DR OrthoDB; 1107373at2; -.
DR EvolutionaryTrace; Q9RUZ0; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
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..284
FT /note="Citrate lyase subunit beta-like protein"
FT /id="PRO_0000286387"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:1SGJ"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:1SGJ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1SGJ"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:1SGJ"
SQ SEQUENCE 284 AA; 29980 MW; F95B6C9B20F89EC5 CRC64;
MNAPPALLRS VLFAPGNRAD LIAKLPRSAP DAVVIDLEDA VPGTAEAKAA ARPVAHDAAR
DLIAAAPHLA VFVRVNALHS PYFEDDLSVL TPELSGVVVP KLEMGAEARQ VAQMLQERSL
PLPILAGLET GAGVWNAREI MEVPEVAWAY FGAEDYTTDL GGKRTPGGLE VLYARSQVAL
AARLTGVAAL DIVVTALNDP ETFRADAEQG RALGYSGKLC IHPAQVALAH EYFGPTEADR
ARARALLDAA AAAAQRGHGA FSFEGQMVDE PMLAKARTLL SHEA
