ID   A0A372ICE4_9RHOB        Unreviewed;       319 AA.
AC   A0A372ICE4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RFU12577.1};
GN   ORFNames=DZD18_10830 {ECO:0000313|EMBL:RFU12577.1};
OS   Rhodobacteraceae bacterium W635.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU12577.1, ECO:0000313|Proteomes:UP000264655};
RN   [1] {ECO:0000313|EMBL:RFU12577.1, ECO:0000313|Proteomes:UP000264655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W635 {ECO:0000313|EMBL:RFU12577.1,
RC   ECO:0000313|Proteomes:UP000264655};
RA   Hou X.J.;
RT   "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT   lake in Xinjiang province, China.";
RL   Submitted (AUG-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:RFU12577.1}.
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DR   EMBL; QVQC01000053; RFU12577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372ICE4; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000264655; 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:RFU12577.1};
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:UP000264655}.
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;  34159 MW;  C55D4A393A1156DA CRC64;
     MSFRLQPQPP ARPNRCQLFG PGSNTKLFAK MAASDADVIN LDLEDSVAPS DKAQARANVI
     AAIAEHDWGN KTLSVRINGL DTPYWYRDVV DLLEQSDERL DQIMIPKVGC AEDVYAVDAL
     VTAIESATGR GKTIAFEVII ESAAGLAHVA EIAAASPRLQ AMSLGAADFA ASMGMQTTGI
     GGTQENYYML HDGTRHYSDP WHWAQTAIVA ACRTHGLLPV DGPFGDFSDD EGYIAQARRS
     ATLGMVGKWA IHPKQIALAN QVFTPSKEAV MEAREILAAM EAAKEAGEGA TVYKGRLVDI
     ASIKQAEVIV TQAEMIAAG
//