ID Q1LK47_CUPMC Unreviewed; 382 AA.
AC Q1LK47;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Thiolase {ECO:0000313|EMBL:ABF09479.1};
DE EC=2.3.1.176 {ECO:0000313|EMBL:ABF09479.1};
GN OrderedLocusNames=Rmet_2602 {ECO:0000313|EMBL:ABF09479.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF09479.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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; CP000352; ABF09479.1; -; Genomic_DNA.
DR RefSeq; WP_011517182.1; NC_007973.1.
DR AlphaFoldDB; Q1LK47; -.
DR STRING; 266264.Rmet_2602; -.
DR KEGG; rme:Rmet_2602; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_035425_4_0_4; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00829; SCP-x_thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABF09479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABF09479.1}.
FT DOMAIN 24..181
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..350
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 382 AA; 39918 MW; 9483529AF9F93725 CRC64;
MNRLLQQTSV YVIGVGLHPY QFASDTPYVS LGLRAMREAL SDAGIAWPEV QSAYVGTSAI
GMATGRVMFR HLGSTGLAVT QVESASASGC SAFRQACLEV ASGVSDVVVA IGVDKFGDGR
KAADKDGLPH LAPTATMPPV KFALMAHEYL RQHGLKPEAM ARVAVKNHGN AALNPYAQFR
KARTLEQVMA SPKVVGDLTV QQCCPRGDGA AAVIVVSEAA IKRLGLDKRR AVRVLASVAN
SEELEHGDSS AAVDMVRKST AMAYEQAGVG PRDLNLVELH EAFSIEELVY TEAMDLCAPG
EGAAWLERGA SAIGGECAVN ASGGLLGMGH PTGPTGIGQI AEITRQIRGE AHGRQHPGAR
LGLAHMIGLG SVAFAHILAA SH
//
