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Database: UniProt
Entry: A0A2C6DFA2_9GAMM
LinkDB: A0A2C6DFA2_9GAMM
Original site: A0A2C6DFA2_9GAMM 
ID   A0A2C6DFA2_9GAMM        Unreviewed;       291 AA.
AC   A0A2C6DFA2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:PHI29866.1};
GN   ORFNames=CRN84_11185 {ECO:0000313|EMBL:PHI29866.1};
OS   Budvicia aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Budvicia.
OX   NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI29866.1, ECO:0000313|Proteomes:UP000224974};
RN   [1] {ECO:0000313|Proteomes:UP000224974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:PHI29866.1}.
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DR   EMBL; PDDX01000001; PHI29866.1; -; Genomic_DNA.
DR   RefSeq; WP_029096531.1; NZ_PDDX01000001.1.
DR   AlphaFoldDB; A0A2C6DFA2; -.
DR   STRING; 1111728.GCA_000427805_01828; -.
DR   OrthoDB; 6831788at2; -.
DR   Proteomes; UP000224974; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:PHI29866.1};
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:UP000224974}.
FT   DOMAIN          5..220
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         125
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"
SQ   SEQUENCE   291 AA;  31361 MW;  4E55EF54E8BCFF4A CRC64;
     MDLLRTLLFL PGNNPGMLQN GGVFGSDAVI LDLEDAVSPQ EKDAARYLIG YALRHINYRK
     SKRVVRINPL DCGGADDIAA MVPCGPDALM LPKIDTAEEL RQIIELIERA EQPGQTPVRV
     IPLLETPQSI IHAYDIACAH PRVWAISFGA EDYTAALGAI RSRSGEEILS ARTAVVNAAA
     AAGIDSIDTP FTDAQDDDGL LQDSLLARGL GFKGKLAINP RQVDTIHQAF SPTSADIHWA
     KRVVHALDEA KVLGSGVIAL DGKMVDAPIV LRAERTLKLA AYLNLQQEDM A
//
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