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
//