ID   A0A2I6S799_9RHOO        Unreviewed;       330 AA.
AC   A0A2I6S799;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:AUN95137.1};
GN   ORFNames=C0099_09420 {ECO:0000313|EMBL:AUN95137.1};
OS   Pseudazoarcus pumilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Pseudazoarcus.
OX   NCBI_TaxID=2067960 {ECO:0000313|EMBL:AUN95137.1, ECO:0000313|Proteomes:UP000242205};
RN   [1] {ECO:0000313|EMBL:AUN95137.1, ECO:0000313|Proteomes:UP000242205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY39 {ECO:0000313|EMBL:AUN95137.1,
RC   ECO:0000313|Proteomes:UP000242205};
RA   Fu G.-Y.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP025682; AUN95137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I6S799; -.
DR   KEGG; atw:C0099_09420; -.
DR   OrthoDB; 8481499at2; -.
DR   Proteomes; UP000242205; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.960; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR040186; Citramalyl-CoA_lyase.
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; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:AUN95137.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242205}.
FT   DOMAIN          50..243
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   330 AA;  36384 MW;  BEA1C5C64ECF8497 CRC64;
     MTDRNHPAEV LFDAEKPFPV LPAVDHYAGA EKLMRKALAL QAELGPVFDV TFDCEDGAHA
     GAESEHATMA AELAAGGDNR FGRVGARIHD ITHALWRQDL DILVRGAGHR LAFVTLPKAR
     SAADVRDQVQ ALRAIEAEHG VTRAIPVHVL IETHGALREI WQIAALEGVE SVDFGIMDFV
     SAHHGALSGA EMVSPGQFTH PLIVRAKTEI VAAALANGVV PAHNVTTELR DIERIGDDAR
     RARREFGFLR MWSIHPNQIQ PIVDAMRPDY SEVSAAAEIL IAAQEASWGP IQHAGKLHDR
     ASYRYYWELL VRARTTGMEI DTEARRRFFD
//