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Database: UniProt
Entry: A0A0F0L2M3_9MICO
LinkDB: A0A0F0L2M3_9MICO
Original site: A0A0F0L2M3_9MICO 
ID   A0A0F0L2M3_9MICO        Unreviewed;       291 AA.
AC   A0A0F0L2M3; A0A1I6HYQ0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SFR59596.1};
DE   SubName: Full=Citrate lyase subunit beta-like protein {ECO:0000313|EMBL:KJL27392.1};
DE            EC=4.1.-.- {ECO:0000313|EMBL:KJL27392.1};
GN   ORFNames=RL72_00487 {ECO:0000313|EMBL:KJL27392.1}, SAMN04488591_2275
GN   {ECO:0000313|EMBL:SFR59596.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL27392.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL27392.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL27392.1,
RC   ECO:0000313|Proteomes:UP000033448};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000198877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL127 {ECO:0000313|Proteomes:UP000198877};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFR59596.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL127 {ECO:0000313|EMBL:SFR59596.1};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; JYIT01000053; KJL27392.1; -; Genomic_DNA.
DR   EMBL; FOYR01000002; SFR59596.1; -; Genomic_DNA.
DR   RefSeq; WP_045249231.1; NZ_JYIT01000053.1.
DR   AlphaFoldDB; A0A0F0L2M3; -.
DR   PATRIC; fig|582680.7.peg.502; -.
DR   OrthoDB; 4322898at2; -.
DR   Proteomes; UP000033448; Unassembled WGS sequence.
DR   Proteomes; UP000198877; Unassembled WGS sequence.
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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KJL27392.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT   DOMAIN          19..226
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   291 AA;  31348 MW;  69C5EEA36465A0AB CRC64;
     MNAPLPTAGP REIAPELARS WLLVAATKPE TFDEAARSHA DAVVLDVEDA VDASRKDSAR
     DDVVRWLHGA TADGRPNRAW VRINDATSEH WSPDLDGLRD APGLQGVMLA KTEFGGQVMD
     TFNRLGAKVP VVALVESAIG IENATEIARA KGVFRLAFGS GDFRRDTGMS ADREAMAYPR
     ARLVISSRAG GLPGPIDGPT VGSSHPILRE QSAITVSMGM TGKLCLTADQ TPVVNEVISP
     TRTDVEWAYE FLEDFDARGR IVRDGSDLPR LGRARKIMQL AEAFGVLPVT H
//
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