ID A0A328AQZ0_9CAUL Unreviewed; 289 AA.
AC A0A328AQZ0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=CoA ester lyase {ECO:0000313|EMBL:RAK57443.1};
GN ORFNames=DJ018_05750 {ECO:0000313|EMBL:RAK57443.1};
OS Phenylobacterium deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1914756 {ECO:0000313|EMBL:RAK57443.1, ECO:0000313|Proteomes:UP000249725};
RN [1] {ECO:0000313|Proteomes:UP000249725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 73061 {ECO:0000313|Proteomes:UP000249725};
RA Li X.;
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:RAK57443.1}.
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DR EMBL; QFYR01000001; RAK57443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328AQZ0; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000249725; 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:RAK57443.1};
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:UP000249725}.
FT DOMAIN 7..218
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 289 AA; 30271 MW; 4CC9BC700EE5987E CRC64;
MLVRPRRSAL YLPATNARAL EKARTLSCDV VVLDLEDSIA PEAKAEARLA ACEAVRAGGF
GARELVVRIN ALDTPWGAAD LGAVAGAQPD ALLVPKLSDP EDLPAYAAAL GGKTRLWGMI
ETCKAVLRLD ALGAAAAANR MEGWILGLND LAMEMGCRPG ADRAPLQAAM SLAVTAARAH
GLFVLDAVYN DFSDAEGLAR ECAQGVAFGF DGKSLIHPAQ IAAANAAFSP DPEALAWARQ
VVRAFDAPES AGRGVIKVDG KMVERLHLEQ AQRLIALSDA IAVREGSPE
//
