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
//