ID A0A0W7WI89_9RHOB Unreviewed; 319 AA.
AC A0A0W7WI89;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:KUF10254.1};
GN ORFNames=AVJ23_12650 {ECO:0000313|EMBL:KUF10254.1};
OS Pseudoponticoccus marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoponticoccus.
OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF10254.1, ECO:0000313|Proteomes:UP000054396};
RN [1] {ECO:0000313|EMBL:KUF10254.1, ECO:0000313|Proteomes:UP000054396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF10254.1,
RC ECO:0000313|Proteomes:UP000054396};
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:KUF10254.1}.
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DR EMBL; LPXO01000007; KUF10254.1; -; Genomic_DNA.
DR RefSeq; WP_058862572.1; NZ_LPXO01000007.1.
DR AlphaFoldDB; A0A0W7WI89; -.
DR STRING; 1685382.AVJ23_12650; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000054396; 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:KUF10254.1};
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:UP000054396}.
FT DOMAIN 15..253
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 319 AA; 34148 MW; 50AFAE9744324ECE CRC64;
MSFRIQPAAP ARPNRCQLFG PASNTKLPPK MAASAADVIN IDLEDSVAPS DKDMARKLAI
EAIGDVDWGA KTLSVRINGL DTPFWYRDVV DLLEQASERL DQIMIPKVGC AADIYAVDAL
VTAVERAKGR AKPIKFEVII ESAAGIAHVE EIAAASPRLE AMSLGAADFA ASMGMATTGI
GGTQENYYMI REGQKHWSDP WHWAQAAIVA ACRTHGVLPV DGPFGDFSDD DGFRAQALRS
ATLGMVGKWA IHPKQVALAN EVFTPTEEAV ADARAILAAM EEAKARGEGA TTYKGKLIDI
ASIKQAEVIV RQSEMIAGM
//
