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Database: UniProt
Entry: A0A164TD45_9NOCA
LinkDB: A0A164TD45_9NOCA
Original site: A0A164TD45_9NOCA 
ID   A0A164TD45_9NOCA        Unreviewed;       286 AA.
AC   A0A164TD45;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:KZF13238.1};
GN   ORFNames=A2J03_15010 {ECO:0000313|EMBL:KZF13238.1};
OS   Rhodococcus sp. EPR-157.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF13238.1, ECO:0000313|Proteomes:UP000077673};
RN   [1] {ECO:0000313|EMBL:KZF13238.1, ECO:0000313|Proteomes:UP000077673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPR-157 {ECO:0000313|EMBL:KZF13238.1,
RC   ECO:0000313|Proteomes:UP000077673};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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:KZF13238.1}.
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DR   EMBL; LVCV01000016; KZF13238.1; -; Genomic_DNA.
DR   RefSeq; WP_068368194.1; NZ_LVCV01000016.1.
DR   AlphaFoldDB; A0A164TD45; -.
DR   OrthoDB; 5172636at2; -.
DR   Proteomes; UP000077673; 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:KZF13238.1};
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:UP000077673}.
FT   DOMAIN          11..211
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   286 AA;  30176 MW;  7679D082951C3AC4 CRC64;
     MTWSSPGPAW LFCPADRPER FAKAAARADV VILDLEDGVA PADKAAAREA LISTPLDPAT
     TVVRINPQGS ADWSADLAAL DRTDYQIVML PKCEGPQQIA ALAPRLVIAL IESPLGAINS
     YVALGANNAV GAMWGAEDLV AALGGNSSRF NYGGYRDVAQ HVRSQTLLAA KAQGVFALDS
     VFLDIGDLAG LRDEADDAVA VGFDGKVAIH PTQVGVIREA YAPTETEIDW AGRVLAAAKT
     NRGVFSFEGH MVDAPVIQHA RRILARVREG DVRRADQSLS PGAVDA
//
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