ID   A0A0B2BLC3_9ACTN        Unreviewed;       294 AA.
AC   A0A0B2BLC3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Citrate lyase subunit beta/citryl-CoA lyase {ECO:0000313|EMBL:PJJ56344.1};
GN   ORFNames=CLV56_0550 {ECO:0000313|EMBL:PJJ56344.1};
OS   Mumia flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Mumia.
OX   NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ56344.1, ECO:0000313|Proteomes:UP000230842};
RN   [1] {ECO:0000313|EMBL:PJJ56344.1, ECO:0000313|Proteomes:UP000230842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ56344.1,
RC   ECO:0000313|Proteomes:UP000230842};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJJ56344.1}.
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DR   EMBL; PGEZ01000001; PJJ56344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2BLC3; -.
DR   OrthoDB; 5172636at2; -.
DR   Proteomes; UP000230842; 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:PJJ56344.1};
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:UP000230842}.
FT   DOMAIN          4..232
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   294 AA;  30554 MW;  B8A193166004C243 CRC64;
     MVARSYLYVP ATAGDKLAKV LQRGADAVIV DLEDAVPFPA KDGARADVVA WLEGLDGRSD
     VDRRPAGPPD VEIWVRLNAG EPGLVDAAAV AAPRVAGVML AKTETREEID ALDAVLTDAE
     QRRGLPSGSI GVVPLLESAA ALLRAPAIAA GPRVVRLQVG EADLAADLGF GEDADDADWA
     PIRSQIVVTS AAAGISAPVA PVSTDFRDLD ALAASTRALA RRGYVGRACI HPAQVSVVND
     VFTPSEQRLA AARALIATFD RAVEAGQGVI VGPDGRMIDE AVVRRARNLV ALAR
//