ID A0A1A9N8V3_9BURK Unreviewed; 394 AA.
AC A0A1A9N8V3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN ORFNames=A6V37_24340 {ECO:0000313|EMBL:OAJ61823.1};
OS Paraburkholderia ginsengiterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ61823.1, ECO:0000313|Proteomes:UP000078116};
RN [1] {ECO:0000313|EMBL:OAJ61823.1, ECO:0000313|Proteomes:UP000078116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY85 {ECO:0000313|EMBL:OAJ61823.1,
RC ECO:0000313|Proteomes:UP000078116};
RA Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAJ61823.1}.
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; LXKA01000198; OAJ61823.1; -; Genomic_DNA.
DR RefSeq; WP_064272526.1; NZ_LXKA01000198.1.
DR AlphaFoldDB; A0A1A9N8V3; -.
DR STRING; 1462993.A6V36_16585; -.
DR OrthoDB; 9785768at2; -.
DR Proteomes; UP000078116; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
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; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..112
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..369
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 394 AA; 41760 MW; 3F0DE5DF871FCF7F CRC64;
MSQNVYVAGV GMIPFTKPGA SEAYYQMGAK AAVAALDDAG VGYDQIDHAY AGFMYADSCA
GQRALYEVGM TGIPVFNVNN NCATGSTAIY LARQAIEAGA AECILMVGFD QMVPGALEVQ
FKDRPSVFDR FYAAIDEKLG ASEVPGALRI FGSAGLAHME RFGTRLETFA KIRAKASRHA
ANNPLAVFRN VVSTEEVMAS PMVWPGVMTR LMACPPTCGA AAAVLCSEDF ASRHGLKRDV
RIAAQAMTTD RANAFDGVDM REVAGFSMSR TAAQKVYEQA GVGPQDIDVV ELHDCFAQNE
LLTYEALGLC PEGGAEKFVD DGDNTYGGQV VTNPSGGLLS KGHPLGATGL AQCHELVSQL
RCKAAKRQVE GARLALQHNI GIGGACVVTL YERT
//
