ID A0A0X3UEC0_9RHOB Unreviewed; 325 AA.
AC A0A0X3UEC0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:KUJ85136.1};
GN ORFNames=AVO45_17965 {ECO:0000313|EMBL:KUJ85136.1};
OS Ruegeria marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ85136.1, ECO:0000313|Proteomes:UP000053791};
RN [1] {ECO:0000313|EMBL:KUJ85136.1, ECO:0000313|Proteomes:UP000053791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ85136.1,
RC ECO:0000313|Proteomes:UP000053791};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUJ85136.1}.
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DR EMBL; LQBQ01000004; KUJ85136.1; -; Genomic_DNA.
DR RefSeq; WP_068345044.1; NZ_LQBQ01000004.1.
DR AlphaFoldDB; A0A0X3UEC0; -.
DR STRING; 1685379.AVO45_17965; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000053791; 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:KUJ85136.1};
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:UP000053791}.
FT DOMAIN 16..259
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 325 AA; 35705 MW; 065A555856E33452 CRC64;
MSFHSFEQAP ARLNRSELAV PGSQPQMFEK AAQSEVDVIF LDLEDAVAPD EKEQARRNII
KALNEIDWGN KTMSVRINGL DTHYMYRDVV DVVEQAGERL DLIMIPKVGT AADVYAVDMM
VTQIEDARGY KKRIGFEHII ETALGMQNVH EIAAASKRNE SLHFGVADYA ASTRARTTII
GGVNPDYSVL TDPLEDGSRD VHWGDMWHYA LARMVVAARA NGLRPIDGPF GDFQDPEGYR
AAARRAAVLG CEGKWAIHPS QIVLANEVMS PSEAEITKAN RILAAMAEAE AAGKGAVSLD
GRLIDYASIR QAEVLVEKAR RIAAE
//
