ID A0A078L0J3_9GAMM Unreviewed; 282 AA.
AC A0A078L0J3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:CDZ77523.1};
GN Name=mcl1 {ECO:0000313|EMBL:CDZ77523.1};
GN ORFNames=BN59_01806 {ECO:0000313|EMBL:CDZ77523.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ77523.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ77523.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) 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; CCSB01000002; CDZ77523.1; -; Genomic_DNA.
DR RefSeq; WP_043874049.1; NZ_CCVW01000002.1.
DR AlphaFoldDB; A0A078L0J3; -.
DR STRING; 1034943.BN59_01806; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 6831788at2; -.
DR Proteomes; UP000044071; 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:CDZ77523.1};
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:UP000044071}.
FT DOMAIN 9..219
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 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 282 AA; 30973 MW; 74E13F3DA7AAEB68 CRC64;
MDLSIAPALL FTPGNKPERF AKGLNSGANG LILDLEDAVP EAEKEQARDN VLQFLNGETP
DSVYTIIRIN HIKTNAGLRD LLALKDADYH CDAILYPKTE SAEELKIIYE LLNLEARNIK
LLALIETTKG ANQISATVNA APFLAGLVFG AADYCADAGC ELTWESLLFP RYQVVQAAAL
AKIAAIDSPF FDFANEEKLV SETMEVKALG FKGKLAIHPK QVDAIKRCFT PSAEQVEKAR
KIIALYEEAG GKACQYQGEM IDVPVYRHAQ QLVQLFKSIR GE
//