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Database: UniProt
Entry: U5EBP2_NOCAS
LinkDB: U5EBP2_NOCAS
Original site: U5EBP2_NOCAS 
ID   U5EBP2_NOCAS            Unreviewed;       272 AA.
AC   U5EBP2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Putative citrate lyase beta subunit {ECO:0000313|EMBL:GAD83836.1};
GN   ORFNames=NCAST_20_04060 {ECO:0000313|EMBL:GAD83836.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD83836.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD83836.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD83836.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(2014).
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:GAD83836.1}.
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DR   EMBL; BAFO02000020; GAD83836.1; -; Genomic_DNA.
DR   RefSeq; WP_019049331.1; NZ_VBUS01000001.1.
DR   AlphaFoldDB; U5EBP2; -.
DR   STRING; 1824.SAMN05444423_1011141; -.
DR   eggNOG; COG2301; Bacteria.
DR   OrthoDB; 5172636at2; -.
DR   Proteomes; UP000017048; 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:GAD83836.1};
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:UP000017048}.
FT   DOMAIN          12..212
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   272 AA;  29085 MW;  9C2313F02C1237E0 CRC64;
     MSAWEPAGPA WLFCPADRPE RFAKAAAVAD VVILDLEDGV AAADKAAAKK ALIETPLDPE
     RTVVRVNAAD TDEYPADLAA LAQTAYRRVM LPKCEAAEQV RSLTGYEVIV LVESPLGAVR
     VAETVAVDNA VGVMWGAEDL VAGLGGNSSR HADGGYRDVA RHVRSSSLLA AKAFGRFALD
     SVFLDIENLE GLAVETLDAV AVGFDAKVAI HPRQVAVIRE GYAPDPDELD WARRVLAAVP
     NHRGVFAFEG RMVDAPVLRH AERIVRRAEL SG
//
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