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Database: UniProt
Entry: A0A328BLW7_9CAUL
LinkDB: A0A328BLW7_9CAUL
Original site: A0A328BLW7_9CAUL 
ID   A0A328BLW7_9CAUL        Unreviewed;       288 AA.
AC   A0A328BLW7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RAK67665.1};
GN   ORFNames=DJ019_07120 {ECO:0000313|EMBL:RAK67665.1};
OS   Phenylobacterium kunshanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=1445034 {ECO:0000313|EMBL:RAK67665.1, ECO:0000313|Proteomes:UP000249524};
RN   [1] {ECO:0000313|EMBL:RAK67665.1, ECO:0000313|Proteomes:UP000249524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUT-10 {ECO:0000313|EMBL:RAK67665.1,
RC   ECO:0000313|Proteomes:UP000249524};
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA   Winkler M.E.;
RL   Submitted (MAY-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:RAK67665.1}.
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DR   EMBL; QFYS01000002; RAK67665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328BLW7; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000249524; 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:RAK67665.1};
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:UP000249524}.
FT   DOMAIN          8..219
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         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   288 AA;  29898 MW;  F0140BD43EFDCC43 CRC64;
     MTSARPRRSA LYLPASNARA VEKARALACD VVILDLEDAV APDAKDEARA GAVAAARAAG
     FGPRELVIRV NGLDTPWGEA DLAAATEARP DAVLIPKVSS PDDIAAARAR APSDIPLWAM
     IETCAAMFRL EALGAASRHA GVAAWVIGSN DLAKEMRCAL DAERAPLATA LSLSLMAARA
     HGLTILDGVY NDIADADGLA RQCAQGAALG FDGKTLIHPS QVDAANAAFS PDADAVAWAR
     TVVTAFDAPE AVGRGVIKVE GRMVERLHLE QARRLIAVAD AIEARTAG
//
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