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
//