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Database: UniProt
Entry: A0A3R9PB65_9RHOB
LinkDB: A0A3R9PB65_9RHOB
Original site: A0A3R9PB65_9RHOB 
ID   A0A3R9PB65_9RHOB        Unreviewed;       319 AA.
AC   A0A3R9PB65;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RSK32744.1};
GN   ORFNames=EJA01_10415 {ECO:0000313|EMBL:RSK32744.1};
OS   Rhodovulum robiginosum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK32744.1, ECO:0000313|Proteomes:UP000275159};
RN   [1] {ECO:0000313|EMBL:RSK32744.1, ECO:0000313|Proteomes:UP000275159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK32744.1,
RC   ECO:0000313|Proteomes:UP000275159};
RA   Gupta D., Guzman M.S., Bose A.;
RT   "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT   robiginosum.";
RL   Submitted (DEC-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:RSK32744.1}.
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DR   EMBL; RWGU01000048; RSK32744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9PB65; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000275159; 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:RSK32744.1};
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:UP000275159}.
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;  34557 MW;  F167D6049C273FAE CRC64;
     MSFRIQPTPV SRPNRCQLFG PGSRPQIFEK MAASEADVIN LDLEDSVAPD DKDSARRNVI
     EAIGDIDWGK KHLSVRINGL DTPYWYRDVV ELLENASDRL DQIMIPKAGC GADIYAVDAL
     VTAVERAKGR TKPIGFEVII ESAAGIAHVE EIAAASPRMQ AMSLGAADFA ASMGMATTGI
     GGTQENYYMH REGERYWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDD EGFRAQARRS
     ATLGMVGKWA IHPKQVALAN EVFTPSDEAV AEAREILAAM EKAKAEGAGA TVYKGRLVDI
     ASIKQAEVIV QQAEMIAGR
//
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