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Database: UniProt
Entry: A0A1G8GY68_9MICO
LinkDB: A0A1G8GY68_9MICO
Original site: A0A1G8GY68_9MICO 
ID   A0A1G8GY68_9MICO        Unreviewed;       294 AA.
AC   A0A1G8GY68;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SDH99294.1};
GN   ORFNames=SAMN04489720_3122 {ECO:0000313|EMBL:SDH99294.1};
OS   Agrococcus jejuensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=399736 {ECO:0000313|EMBL:SDH99294.1, ECO:0000313|Proteomes:UP000198822};
RN   [1] {ECO:0000313|EMBL:SDH99294.1, ECO:0000313|Proteomes:UP000198822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22002 {ECO:0000313|EMBL:SDH99294.1,
RC   ECO:0000313|Proteomes:UP000198822};
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; LT629695; SDH99294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8GY68; -.
DR   STRING; 399736.SAMN04489720_3122; -.
DR   Proteomes; UP000198822; Chromosome i.
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:SDH99294.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          9..210
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   REGION          261..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         111
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"
SQ   SEQUENCE   294 AA;  30546 MW;  5E554B41BFDAC422 CRC64;
     MIFEMGPALL FCPGDRPDRF AKAAERADAV ILDLEDAVGP DAKAAAREAI ASASLDPAMT
     IVRVNAIGEG MLEADLDAAR RAGVTTIMLA KAESPRQLDA LDGFAVIALC ETAAGVVHAV
     DIAAHPNVVA LMWGAEDLVA SLGGTSSRDE TGAYRAVATH ARSHVLLAAA ASGKRAIDAI
     RTDIADVDGC RVEAIDASAS GFFAKAAIHP AHVAPIREAF APSADEAAWA ERVLAAAAEH
     PGVFSFEGRM VDEPILRHAR SVRARAASDP LPTRQDPAEP DEGTDAPRAH EEAS
//
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