ID   A0A1N6JA84_9RHOB        Unreviewed;       286 AA.
AC   A0A1N6JA84;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=(3S)-malyl-CoA thioesterase {ECO:0000313|EMBL:SIO41046.1};
GN   ORFNames=SAMN05444722_1964 {ECO:0000313|EMBL:SIO41046.1};
OS   Rhodovulum sp. ES.010.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1882821 {ECO:0000313|EMBL:SIO41046.1, ECO:0000313|Proteomes:UP000184943};
RN   [1] {ECO:0000313|EMBL:SIO41046.1, ECO:0000313|Proteomes:UP000184943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES.010 {ECO:0000313|EMBL:SIO41046.1,
RC   ECO:0000313|Proteomes:UP000184943};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FSRS01000001; SIO41046.1; -; Genomic_DNA.
DR   RefSeq; WP_074219921.1; NZ_FSRS01000001.1.
DR   AlphaFoldDB; A0A1N6JA84; -.
DR   STRING; 1882821.SAMN05444722_1964; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000184943; 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:UP000184943}.
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   286 AA;  30803 MW;  D5946A3C5EDFAAC5 CRC64;
     MDPRARPFRS VLYIPGSKAR ALEKARTLPV DAIIFDLEDA VAIEEKPAAR TLLAETLAGN
     DYGTRYRIVR VNGLETEWGH DDLAAIRRAG ADAVLLPKVE TTAQLDALAE AVPGVPLWAM
     METPKGILNA DALAAHPRLE GFVMGTNDLA KEIGCRARPD RLPLMASLTH CLLAARAHGI
     VAVDGVYNAF RDEDGLRDEC EQGRDLGFDG KSLIHPAQVA VANESFAPTE EEIDLAERQI
     AAYDEAERAG QGVAVVDGRI VENLHIVTAR DTLAKAGRIA ELEAAS
//