ID A0A126V5J6_9RHOB Unreviewed; 284 AA.
AC A0A126V5J6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Malyl-CoA thiolesterase {ECO:0000313|EMBL:AML53611.1};
GN ORFNames=RC74_09365 {ECO:0000313|EMBL:AML53611.1};
OS Falsihalocynthiibacter arcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsihalocynthiibacter.
OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML53611.1, ECO:0000313|Proteomes:UP000070371};
RN [1] {ECO:0000313|EMBL:AML53611.1, ECO:0000313|Proteomes:UP000070371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML53611.1};
RA Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT arctic marine sediment.";
RL Submitted (FEB-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; CP014327; AML53611.1; -; Genomic_DNA.
DR RefSeq; WP_039001418.1; NZ_CP014327.1.
DR AlphaFoldDB; A0A126V5J6; -.
DR STRING; 1579316.RC74_09365; -.
DR KEGG; hat:RC74_09365; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000070371; Chromosome.
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:UP000070371}.
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; 30456 MW; B62A7ADB0515AF39 CRC64;
MPVETSLTRS VLYIPASKER ALEKARGLET DAIIFDLEDA VAPDEKETAR AVLRKALTQG
GYGSRLRIVR INGAETEWGK ADIEALKTMD FDAVLLPKVE SAADISNVNS ALPDVPVWAM
IETPKGILHA EEIAVHPALE GFVMGTNDLA KELRCRFRAD RLPLIGALQS ALLAARAHGV
IAIDGVYNAF KDDAGLALEC EQGRDLGFDG KTLIHPAQLA TANRVFSPSA AEVDLANRQI
EAYETAEAVG QGVAVVDGKI VENLHVVTAR QVLSQAKAIA EAQE
//
