ID G5SGS0_SALET Unreviewed; 280 AA.
AC G5SGS0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000313|EMBL:EHC99885.1};
GN ORFNames=LTSEWAN_4751 {ECO:0000313|EMBL:EHC99885.1};
OS Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC99885.1, ECO:0000313|Proteomes:UP000003536};
RN [1] {ECO:0000313|EMBL:EHC99885.1, ECO:0000313|Proteomes:UP000003536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-580 {ECO:0000313|EMBL:EHC99885.1,
RC ECO:0000313|Proteomes:UP000003536};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC99885.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFCX01001549; EHC99885.1; -; Genomic_DNA.
DR AlphaFoldDB; G5SGS0; -.
DR SMR; G5SGS0; -.
DR PATRIC; fig|913086.3.peg.3660; -.
DR Proteomes; UP000003536; 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 NCBIfam; NF038242; RipC_Ccl; 1.
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:EHC99885.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 10..222
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 280 AA; 29912 MW; 304CACB2748C2C36 CRC64;
MPDISHTPTR SWLFTPAIRP ERFIKAVESA ADISIIDLED SVTPNDKAQA RKIAMQFLSS
RPNSSLKIAL RINGMNTHAG IEDLHMLLEC RFFPDYIILP KTESAAHLQI VDSLIMMAGS
DTRLIGIIES VVGLNAVESI ADATPRLCGL MFGAADMAAD IGATPAWEPL ALARARIVAA
CAMKGLLAID APFFDIGDFS GLKEETLQAL SFGFSAKSAI HPAQISVINA AFTPTTAEIN
HARAVLTENA KGVGIVSGMM IDAAVARQAR RLLARAGIFS
//
