ID   A0A2U2CKP4_9RHOB        Unreviewed;       318 AA.
AC   A0A2U2CKP4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PWE32412.1};
GN   ORFNames=DDZ14_10110 {ECO:0000313|EMBL:PWE32412.1};
OS   Maritimibacter sp. 55A14.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=2174844 {ECO:0000313|EMBL:PWE32412.1, ECO:0000313|Proteomes:UP000245064};
RN   [1] {ECO:0000313|EMBL:PWE32412.1, ECO:0000313|Proteomes:UP000245064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55A14 {ECO:0000313|EMBL:PWE32412.1,
RC   ECO:0000313|Proteomes:UP000245064};
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA   Winkler M.E.;
RL   Submitted (MAY-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:PWE32412.1}.
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DR   EMBL; QEYE01000010; PWE32412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2CKP4; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000245064; 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:PWE32412.1};
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:UP000245064}.
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   318 AA;  34455 MW;  A03554CE552E8B77 CRC64;
     MSFRIQPQPP ARPNRCQLFG PGSNPKLFEK MAASEADVIN IDLEDSVAPG DKDAALRNTI
     QAINDVDWGR KTLSVRINGL DSPFWYRDVV DLLEQAGERL DQIMIPKAGC AADIYAVDAL
     VTSIEAAKGR KKRIAFEVII ESAAGIAHVE EIAAASPRLA AMSLGAADFA ASMGMQTTGI
     GGTQENYYML HDGQKHWSDP WHWAHVAIVA ACRTHGLLPV DGPFGDFSDD DGFRAQAWRS
     ATLGMVGKWA IHPKQIALAN EVFTPSDAAV TEAREILQAM EDAKARGEGA TTYKGRLVDI
     ASIKQAEVVV KQAEMISR
//