ID S6ANC9_PSERE Unreviewed; 382 AA.
AC S6ANC9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative acetyl-CoA acyltransferase {ECO:0000313|EMBL:BAN47078.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:BAN47078.1};
GN ORFNames=PCA10_13460 {ECO:0000313|EMBL:BAN47078.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN47078.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN47078.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN47078.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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; AP013068; BAN47078.1; -; Genomic_DNA.
DR RefSeq; WP_016491280.1; NC_021499.1.
DR AlphaFoldDB; S6ANC9; -.
DR STRING; 1245471.PCA10_13460; -.
DR KEGG; pre:PCA10_13460; -.
DR PATRIC; fig|1245471.3.peg.1361; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000015503; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:BAN47078.1}.
FT DOMAIN 5..251
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..381
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 382 AA; 41227 MW; ACC9B383B7FDDA2F CRC64;
MPQAYIVDAL RTPTGRRKGG LSQIHAADLG AHVLRELVAR NGIPEEDYDD VIFGCVDTIG
PLAGDIARTC WLAAGLHQAV PGTTIDRQCG SSQQAVHFAA QAVMSGTQDV VIAGGVQTMT
QIPISSAMTA AEPLGFSDPF SGSEGWVKRY GRVPPTQFRA AQMIAEKWQL SREALEAYAL
ESHRRALRAI EQGRFAREIV PLAGVEHDET PRQTSLDKMA ELETLFGCDR VTAAVSSQTC
DGASALLVVS EAALKRYDLT PRARIQHISV RADDPVWMLT APIPATEYAL KRAGMKLEDI
DRVEINEAFA SVAMAWLKET GYPHERTNVN GGAIALGHPL GATGTRLMCT LLHELERSGG
RFGLQTMCEG GGQANVTIIE RL
//
