ID A0A1X1YRX6_9MYCO Unreviewed; 399 AA.
AC A0A1X1YRX6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AWC16_03250 {ECO:0000313|EMBL:ORW13795.1};
OS Mycolicibacter longobardus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=1108812 {ECO:0000313|EMBL:ORW13795.1, ECO:0000313|Proteomes:UP000193866};
RN [1] {ECO:0000313|EMBL:ORW13795.1, ECO:0000313|Proteomes:UP000193866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45394 {ECO:0000313|EMBL:ORW13795.1,
RC ECO:0000313|Proteomes:UP000193866};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-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:ORW13795.1}.
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DR EMBL; LQPG01000007; ORW13795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1YRX6; -.
DR STRING; 1108812.AWC16_03250; -.
DR OrthoDB; 9785768at2; -.
DR Proteomes; UP000193866; 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; 2.
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..230
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..368
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 399 AA; 42649 MW; 92C6DF3A6F3AC2FF CRC64;
MSNRVFVVGV GMTKFEKPGR REGWDYPAMA KESGTKALED AGIEYGQIQE AAAGYVYGDS
TSGERAIYEL GMTGIPVVNV NNNCSTGSSA LYLAARAIRG GLADCALAIG FEKMQSGSLD
AGFSDREQPL LRHIEALAQL RDFAMPVAPW MFGAAGAEHM EQFGSTPEHY AKIAEKNHRH
SANNPYAQFQ DVYTLEEIQS AKMVYEPLQM TRLMCSPTSD GSGAAVLASE RFVEEHDLAD
RAVEIVGQSL VTDTESTFSA KTARALVGYD MSATAARNVY EQAGIAPDDV DVIELHDCFA
PNELLTYEAL GLCAEGEGHK LVDAGDTTYG GRWVVNPSGG LISKGHPLGA TGLAQCAEMT
WQLRGQADAR QVPNAQVALA HNIGLGGAAV VTAYRPAQR
//
