ID A0A1I6GXN7_9RHOB Unreviewed; 280 AA.
AC A0A1I6GXN7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=(3S)-malyl-CoA thioesterase {ECO:0000313|EMBL:SFR46962.1};
GN ORFNames=SAMN04488005_2310 {ECO:0000313|EMBL:SFR46962.1};
OS Yoonia tamlensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=390270 {ECO:0000313|EMBL:SFR46962.1, ECO:0000313|Proteomes:UP000199478};
RN [1] {ECO:0000313|Proteomes:UP000199478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26879 {ECO:0000313|Proteomes:UP000199478};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOYP01000001; SFR46962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6GXN7; -.
DR STRING; 390270.SAMN04488005_2310; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000199478; 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:UP000199478}.
FT DOMAIN 7..211
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 280 AA; 29141 MW; 40481D20F70C375F CRC64;
MHTRPFRSAL YIPGSKPRAL DKARGLPVDA ILFDLEDAVS PDAKAEARST LADALAQGGY
GPRLKIVRMN GLDTDWGADD AAAIAAMDCD AVLLPKVNSV ADLDALAALI PDLPIWAMME
TPQGILNAAS IAAHPRMAGF VLGTNDLAKD LHARGRAAMV TSLQLCVLAA KAAGIVVLDG
VYNAFKDDDG LRAECAQGRD MGFDGKTLIH PAQIAITNAA FGPSAEDIDL ARRQIAAFDA
AAAEGQGVAV VDGRIVENLH IVTARATLAK ADAIAALETT
//