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
//