ID   A0A1H8VGF5_9RHOB        Unreviewed;       284 AA.
AC   A0A1H8VGF5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=(3S)-malyl-CoA thioesterase {ECO:0000313|EMBL:SEP14481.1};
GN   ORFNames=SAMN04490248_12911 {ECO:0000313|EMBL:SEP14481.1};
OS   Salinihabitans flavidus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salinihabitans.
OX   NCBI_TaxID=569882 {ECO:0000313|EMBL:SEP14481.1, ECO:0000313|Proteomes:UP000198893};
RN   [1] {ECO:0000313|EMBL:SEP14481.1, ECO:0000313|Proteomes:UP000198893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27842 {ECO:0000313|EMBL:SEP14481.1,
RC   ECO:0000313|Proteomes:UP000198893};
RA   de Groot N.N.;
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; FODS01000029; SEP14481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8VGF5; -.
DR   STRING; 569882.SAMN04490248_12911; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000198893; 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:UP000198893}.
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   284 AA;  30472 MW;  095BF77B2E486F9E CRC64;
     MDQRNRPFRS VLYIPASKER ALDKARSLPV DAIIFDLEDA VAVEEKANAR GILAEALAAK
     GYGARMRIVR INGLESDWGR ADAQAARDMG CDAVLLPKVE SAAQVQALAE IVGEIPIWAM
     METPRGMLNA AEIAAYPRMA GFVMGTNDLA KELQTRFRPD RQPLMAGLGL CLLAAKAEGL
     VIVDGVYNAF KDDEGLRAEC AQGRDMGFDG KTLIHPAQVE IANAAFAPTQ DEIDLARRQI
     AAFEEAESSG KGVAVVDGRI VENLHVATAR EILAKADAIT AISG
//