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Database: UniProt
Entry: A0A347UJI5_9RHOB
LinkDB: A0A347UJI5_9RHOB
Original site: A0A347UJI5_9RHOB 
ID   A0A347UJI5_9RHOB        Unreviewed;       281 AA.
AC   A0A347UJI5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:AXX99013.1};
GN   ORFNames=BAR1_14395 {ECO:0000313|EMBL:AXX99013.1};
OS   Profundibacter amoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Profundibacter.
OX   NCBI_TaxID=2171755 {ECO:0000313|EMBL:AXX99013.1, ECO:0000313|Proteomes:UP000261704};
RN   [1] {ECO:0000313|EMBL:AXX99013.1, ECO:0000313|Proteomes:UP000261704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAR1 {ECO:0000313|EMBL:AXX99013.1,
RC   ECO:0000313|Proteomes:UP000261704};
RA   Le Moine Bauer S., Sjoeberg A.G., L'Haridon S., Stokke R., Roalkvam I.,
RA   Steen I.H., Dahle H.;
RT   "Profundibacter amoris BAR1 gen. nov., sp. nov., a new member of the
RT   Roseobacter clade isolated at Lokis Castle Vent Field on the Arctic Mid-
RT   Oceanic Ridge.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP032125; AXX99013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A347UJI5; -.
DR   KEGG; pamo:BAR1_14395; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000261704; Chromosome.
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:AXX99013.1};
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:UP000261704}.
FT   DOMAIN          9..213
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   281 AA;  30024 MW;  0CCE8A40E949AD8E CRC64;
     MNTHARPFRS VLYIPASKTR ALEKARGLAT DAIIFDLEDA VAVEEKAAAR GMLADALAQD
     YGARFRIVRI NGLETEWGRE DAAVVGGADA VLLPKVNSAA DVEALAALVG DMPIWAMMET
     PLGILNAAEI AAHSRLRGMV MGTNDLVKDL NCRFRADREP LITSLQMCLL AARAHGVVAV
     DGVYNAFKDD DGLRVECEQG HDMGFDGKTL IHPAQLAVAN EVFAPSEAEV ELARRQIAAF
     EAAEAAGQGV AVVDGRIVEN LHIVTAQQTL AKAKMIAELE G
//
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