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Database: UniProt
Entry: A0A369QWH1_9RHOB
LinkDB: A0A369QWH1_9RHOB
Original site: A0A369QWH1_9RHOB 
ID   A0A369QWH1_9RHOB        Unreviewed;       291 AA.
AC   A0A369QWH1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RDC73458.1};
GN   ORFNames=DLJ49_07815 {ECO:0000313|EMBL:RDC73458.1};
OS   Rhodovulum sp. 12E13.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=2203891 {ECO:0000313|EMBL:RDC73458.1, ECO:0000313|Proteomes:UP000253860};
RN   [1] {ECO:0000313|EMBL:RDC73458.1, ECO:0000313|Proteomes:UP000253860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12E13 {ECO:0000313|EMBL:RDC73458.1,
RC   ECO:0000313|Proteomes:UP000253860};
RA   Zhang R.;
RT   "Rhodovulum sp. nov.,isolated from saltern sediment.";
RL   Submitted (JUL-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:RDC73458.1}.
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DR   EMBL; QPLK01000006; RDC73458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QWH1; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000253860; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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:RDC73458.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253860}.
FT   DOMAIN          5..230
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   291 AA;  30195 MW;  1460C99D78470DFE CRC64;
     MRLTSLLFVP ADSPRKVEKA QGTGAAGVIL DLEDSVAEGA KAAARDGLPG LIAALPAERD
     WALWVRINAL DTGHAEADLA AAIRPGLDGI VLPKAEGGAD VARLAELIAP LEAAAGMAPG
     HVRILPLVTE TPAGLFALST YAPAHPRLAG LTWGAEDLAS VVGATSNRDE TGGWTEPYRL
     ARSLCLFAAA HAGVPAVETL HADFRDADGL AASCRAARRD GFAGRLAIHP AQIEGIERAF
     APTEEEVALA RRIVAAFEAE PHRGAIGIDG KMVDIPHLKQ ARRLLAALGE G
//
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