ID S9R0R1_9RHOB Unreviewed; 283 AA.
AC S9R0R1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=L-malyl-CoA/beta-methylmalyl-CoA lyase {ECO:0000313|EMBL:EPX85513.1};
DE EC=4.1.3.- {ECO:0000313|EMBL:EPX85513.1};
GN ORFNames=Salmuc_04784 {ECO:0000313|EMBL:EPX85513.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX85513.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX85513.1}.
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DR EMBL; APVH01000008; EPX85513.1; -; Genomic_DNA.
DR RefSeq; WP_020038872.1; NZ_KE557273.1.
DR AlphaFoldDB; S9R0R1; -.
DR STRING; 1123237.Salmuc_04784; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000015347; 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:EPX85513.1};
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:UP000015347}.
FT DOMAIN 9..215
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 70
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 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 283 AA; 30171 MW; 2EC8FAD7050B9C2A CRC64;
MDLALRPYRS VLYIPGSKDR ALDKARTLTV DAIIFDLEDA VAPGEKVSAR DTLAAALAQG
GYGRRTRIVR INGLETEWGE ADAKAADAMD CDAILLPKVE STAQLDALAR LTDKPLWAMM
ETPAGILNAQ AIGAHPRLMG MVMGTNDLAK ELSARFRADR LPMMSALGHC LLAAKATDCV
IVDGVYNAFK DDAGLAEECH QGRDMGFDGK TLIHPAQLET ANAAFAPTEA EVELARRQIE
AYEAAEKEGQ GVAVVDGKIV ENLHVATAKS TLAKAEAIAA LSE
//
