ID A0A239WVY8_9FLAO Unreviewed; 402 AA.
AC A0A239WVY8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Beta-ketoadipyl-CoA thiolase {ECO:0000313|EMBL:SNV38429.1};
DE EC=2.3.1.174 {ECO:0000313|EMBL:SNV38429.1};
GN Name=pcaF {ECO:0000313|EMBL:SNV38429.1};
GN ORFNames=SAMEA4412677_00788 {ECO:0000313|EMBL:SNV38429.1};
OS Chryseobacterium taklimakanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=536441 {ECO:0000313|EMBL:SNV38429.1, ECO:0000313|Proteomes:UP000215196};
RN [1] {ECO:0000313|EMBL:SNV38429.1, ECO:0000313|Proteomes:UP000215196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13490 {ECO:0000313|EMBL:SNV38429.1,
RC ECO:0000313|Proteomes:UP000215196};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; LT906465; SNV38429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239WVY8; -.
DR KEGG; ctak:4412677_00788; -.
DR Proteomes; UP000215196; Chromosome 1.
DR GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; 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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:SNV38429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215196};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SNV38429.1}.
FT DOMAIN 5..268
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 277..401
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 402 AA; 42509 MW; A5752A1F77A0FE1E CRC64;
MKNAYITDGT RSAIGNFKGS LAAVRTDDLM ASVIKSLVAK NPDLPLDQIE DVIIGCANQA
GEDNRNVARM ALLLAGLPVT VPGETVNRLC ASGMSAIVQA SRAIKSGEGD LFIAGGVEGM
SRGPYVISKA ENGFDTAQKM YDSSFGWRFI NPEMEKMYGT EAMGKTAENL AEMYQISREE
QDEFALSSQL KAKKAQESGR LAEEISDIMI PQRKGEPIVV SQDEFIKPNS SMEILGKLKP
AFVKENGTVT AGNASGLNDG AAAVIIASGE AVEKYGLKPL AKIVTSAVTG TEPRIMGIGP
VEATKLALKR ANLTLDQIDI IELNEAFAAQ SIAVLKELGL ANDDPRVNVN GGAIALGHPL
GMSGTRITYS AALELQKSGK KYALCTMCVG VGQGYAVILE KA
//
