ID X0RLX3_9GAMM Unreviewed; 504 AA.
AC X0RLX3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:GAF52160.1};
GN ORFNames=JCM18900_1661 {ECO:0000313|EMBL:GAF52160.1};
OS Psychrobacter sp. JCM 18900.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1298608 {ECO:0000313|EMBL:GAF52160.1, ECO:0000313|Proteomes:UP000019500};
RN [1] {ECO:0000313|EMBL:GAF52160.1, ECO:0000313|Proteomes:UP000019500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18900 {ECO:0000313|EMBL:GAF52160.1,
RC ECO:0000313|Proteomes:UP000019500};
RA Kudo T., Kidera A., Kida M., Kawauchi A., Shimizu R., Nakahara T.,
RA Zhang X., Yamada A., Amano M., Hamada Y., Taniyama S., Arakawa O.,
RA Yoshida A., Oshima K., Suda W., Kuwahara H., Nogi Y., Kitamura K., Yuki M.,
RA Iida T., Moriya S., Inoue T., Hongo Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Psychrobacter Strains JCM 18900, JCM 18901, JCM
RT 18902, and JCM 18903, Isolated Preferentially from Frozen Aquatic
RT Organisms.";
RL Genome Announc. 2:e00280-14(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:GAF52160.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAWG01000002; GAF52160.1; -; Genomic_DNA.
DR AlphaFoldDB; X0RLX3; -.
DR eggNOG; COG0183; Bacteria.
DR Proteomes; UP000019500; Unassembled WGS sequence.
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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 83..348
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 360..504
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 53393 MW; 62A00B41D2D30A90 CRC64;
MSNKNNHPDS PVVESTVVKA TDTKSDTAKK ETAAKNTSTK DNSAKDAASK KAVDEKVETT
AAKKPAPAKK ASETKPASNL NRVAILGGNR IPFARSNGSY ADVSNTDMLT AALDGLVERY
NLQGETVGEV VSGAVMKLSR DINLTREATL NTALNPHTPT YDISQACGTG LQATFASANK
IALGLIDSAI TGGVDTTSDA PIAVGDGLRK VLIKLGAAKD NKQRLKALMG LNPKDLIDSP
QNGEPRTGLS MGDHQAITTL EWNISREAQD ELAFNSHQNL ARAYDEGFFD DLITPYKGLT
RDNNLRPDTT LEKLGKLKPV FGRKNANPTM TAANSTPLTD GASCVLLGTD EWAKEHGLKP
LAYIVHQETA AVDFIGKSGT TEGLLMAPAY AVPRMLERAG LTLQDFDFYE IHEAFASQVL
STLAAWEDEK FCEERLGLDA PLGSIDRSKL NVNGSSLAAG HPFAATGGRI LATAAKLLDQ
KGSGRALISI CAAGGQGVTC ILEK
//
