ID J9SBX4_9ACTN Unreviewed; 394 AA.
AC J9SBX4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=KTR9_3195 {ECO:0000313|EMBL:AFR49830.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49830.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR49830.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR49830.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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}.
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DR EMBL; CP002907; AFR49830.1; -; Genomic_DNA.
DR RefSeq; WP_014927443.1; NC_018581.1.
DR AlphaFoldDB; J9SBX4; -.
DR STRING; 337191.KTR9_3195; -.
DR KEGG; gor:KTR9_3195; -.
DR PATRIC; fig|337191.3.peg.3551; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_035425_0_0_11; -.
DR Proteomes; UP000003281; Chromosome.
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, ECO:0000313|EMBL:AFR49830.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 10..192
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..373
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 394 AA; 41252 MW; 0C543F7758BC208B CRC64;
MTNVCISGVG MMPFTKPGKS ETYDRMGATA ARAALADAGL DYTDVQQAYV GYVYGDSTSG
QNALYEIGLT GIPAVNVNNN CSTGSSALWL ARQAVASGTA DCVLALGFEQ MQPGALVNAY
GDRPSPTARG EEIALSRPGG DADAPMAAKM FGGAGVEYMD RHGVTSEVFG RVSVKARTHA
GRNPLAVFRD PIDLDTVMSS KQIWGPLTLL MCCPPTNGAA AAIVCSEEFA RSRGIDSSVR
LRAQSLVTDV AGTFDTTDMM RVAGYDMTAK AAAEVYEQSG VDPLDIPVVE LHDCFSTNEV
ITYEGLGLTP EGTAEKFILD GDNTYGGRVV TNPSGGLLSK GHPLGATGLA QCAELVWQLR
GQAGERQVEG VRIALQHNLG LGGACVVSLY EKVS
//
