ID A0A261VP53_9BORD Unreviewed; 397 AA.
AC A0A261VP53;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CAL24_11520 {ECO:0000313|EMBL:OZI75829.1};
OS Bordetella genomosp. 2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1983456 {ECO:0000313|EMBL:OZI75829.1, ECO:0000313|Proteomes:UP000215633};
RN [1] {ECO:0000313|EMBL:OZI75829.1, ECO:0000313|Proteomes:UP000215633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8256 {ECO:0000313|EMBL:OZI75829.1,
RC ECO:0000313|Proteomes:UP000215633};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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:OZI75829.1}.
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DR EMBL; NEVT01000006; OZI75829.1; -; Genomic_DNA.
DR RefSeq; WP_028356077.1; NZ_NEVT01000006.1.
DR AlphaFoldDB; A0A261VP53; -.
DR Proteomes; UP000215633; 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 8..230
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..374
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 397 AA; 42035 MW; 86301555AD5A0D95 CRC64;
MARQQRPVFV IGVGMIPFTK PGASAPYTVM GAEAAALALE DAGLDYAAVE QAYVGYVYGD
STAGQAAIYG AGLTGIPVFN VNNNCATGSS ALFLARQAVE SGVAECALAL GFEQMTPGAL
KSKYEDRPSP MARFVDAMAS QQGYDAEAPR AAQFFGGAGR AYMREHGIRP DTFGRIAVKA
RQHAARNPLA VFRNVLSLQE VMSSPAIFDP LTRYQCCPPT CGAAAALVCS DDFARRNKLA
RRVRIAAQAM TTDTPSSFES SDMRKLVGYD MTATAARQVY EQAGIGPGDV DVVELHDCFT
TNELITYEGL GLTAEGTAER FILEGDNTYG GRVVTNPSGG LLSKGHPLGA TGLAQCAELY
WQLTGRAEQR QVEGARIALQ HNLGLGGACV VTLYQAV
//