ID   Q8KJG0_RHILI            Unreviewed;       304 AA.
AC   Q8KJG0;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=PROBABLE SIMILAR TO BETA SUBUNIT OF CITRATE LYASE PROTEIN {ECO:0000313|EMBL:CAD31585.1};
GN   Name=msi180 {ECO:0000313|EMBL:CAD31585.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:CAD31585.1};
RN   [1] {ECO:0000313|EMBL:CAD31585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R7A {ECO:0000313|EMBL:CAD31585.1};
RX   PubMed=12003951; DOI=10.1128/JB.184.11.3086-3095.2002;
RA   Sullivan J.T., Trzebiatowski J.R., Cruickshank R.W., Gouzy J., Brown S.D.,
RA   Elliot R.M., Fleetwood D.J., McCallum N.G., Rossbach U., Stuart G.S.,
RA   Weaver J.E., Webby R.J., de Bruijn F.J., Ronson C.W.;
RT   "Comparative sequence analysis of the symbiosis island of Mesorhizobium
RT   loti strain R7A.";
RL   J. Bacteriol. 184:3086-3095(2002).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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DR   EMBL; AL672113; CAD31585.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KJG0; -.
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; Phosphoenolpyruvate-binding domains; 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   PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAD31585.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          19..237
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   304 AA;  32440 MW;  A31FE12F452CDA72 CRC64;
     MIKDTFPAIE SPMSVPRWRS LLFVPAHVPR FVKTAHERGA DGVILDLEDS VPQDRKDQAR
     RQLRGSVAKV GRNGASVLVR VNRGLRALAA DLEAAVVAGV NALVLPKVES AEWVMEVADA
     VTELEHERNL DAGSIRFVAQ IETPGALTRL AAIASAHPRM AAMALGPEDF SAAAGGTPSP
     ELLLGPNLSV LFAARARGLL PLGFVGSIGQ FSDTQKFRDV VIQARRLGFV GALAIHPTQV
     AILNEAFSPS AEEFEWARRV LATERDAAAE GRGAFALDGK MVDAPVVRRA REIIAMGPKA
     ELGV
//