ID   A0A2T8HYR2_9RHOB        Unreviewed;       319 AA.
AC   A0A2T8HYR2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PVH30573.1};
GN   ORFNames=DDE20_03335 {ECO:0000313|EMBL:PVH30573.1};
OS   Pararhodobacter oceanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pararhodobacter.
OX   NCBI_TaxID=2172121 {ECO:0000313|EMBL:PVH30573.1, ECO:0000313|Proteomes:UP000245911};
RN   [1] {ECO:0000313|EMBL:PVH30573.1, ECO:0000313|Proteomes:UP000245911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM505 {ECO:0000313|EMBL:PVH30573.1,
RC   ECO:0000313|Proteomes:UP000245911};
RA   Wang X.-L., Du Z.-J.;
RT   "Pararhodobacter oceanense sp. nov., isolated from marine intertidal
RT   sediment.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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:PVH30573.1}.
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DR   EMBL; QDKM01000001; PVH30573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T8HYR2; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000245911; 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   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:PVH30573.1};
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:UP000245911}.
FT   DOMAIN          15..253
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         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   319 AA;  34618 MW;  02A632F196C3F78C CRC64;
     MSFRIQPPAP ARPNRCQLFG PGSRTALFEK MAVSAADVIN LDLEDSVAPS DKDSARENII
     QATHDVDWNS KYLSVRINGL DTPYWYRDVV DLLENASERL DQIMIPKVGC AADIYAVDAL
     VTAIERAKNR AKPISFEVII ESAAGIAHVE EIAAASKRLQ AMSLGAADFA ASMGMQTTGI
     GGTQENYYML RDGARHWSDP WHWAQTAIVA ACRTHGVLPV DGPFGDFSDD EGFRAQARRS
     ATLGMVGKWA IHPKQIALAN EVFTPSEAAV AEAREILAAM EEAKARGEGA TVYKGRLVDI
     ASIKQAEVIV TQSEMITKG
//