ID A0A0J5QBS8_9RHOB Unreviewed; 285 AA.
AC A0A0J5QBS8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=(3S)-malyl-CoA thioesterase {ECO:0000313|EMBL:KMK66351.1};
GN ORFNames=IMCC21224_111201 {ECO:0000313|EMBL:KMK66351.1};
OS Puniceibacterium sp. IMCC21224.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK66351.1, ECO:0000313|Proteomes:UP000036046};
RN [1] {ECO:0000313|EMBL:KMK66351.1, ECO:0000313|Proteomes:UP000036046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK66351.1,
RC ECO:0000313|Proteomes:UP000036046};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21224 belonging to the
RT Alphaproteobacteria.";
RL Submitted (MAY-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:KMK66351.1}.
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DR EMBL; LDPY01000001; KMK66351.1; -; Genomic_DNA.
DR RefSeq; WP_047994550.1; NZ_LDPY01000001.1.
DR AlphaFoldDB; A0A0J5QBS8; -.
DR STRING; 1618204.IMCC21224_111201; -.
DR PATRIC; fig|1618204.4.peg.1221; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000036046; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 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:UP000036046}.
FT DOMAIN 9..216
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 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 285 AA; 30317 MW; 444D1232B7BDEB40 CRC64;
MDTQTRPFRS VLYLPASNER AMDKARKLPV DAIIFDLEDA VAADEKLRAR DVLDDALAAG
GYGMRMRIVR INGLDSIWGK ADANVVADMD CDAVLLPKVD GPEQIDALAQ HTGDLPIWAM
METPLGMLNA AAIAAHPLVA GMVMGTNDLA KELNSRPRAD RLPMMTGLGL CLLAAKAHGV
VIVDGVYNAF KDEEGLRAEC NLGRDMGFDG KTLIHPAQVD VANAAFGPSV EEIELAQRQI
AAFDAAQSRG EGVAVVDGRI VENLHVATAR VLLAKAAAIE AIAAE
//
