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Database: UniProt
Entry: A4ETV1_9RHOB
LinkDB: A4ETV1_9RHOB
Original site: A4ETV1_9RHOB 
ID   A4ETV1_9RHOB            Unreviewed;       407 AA.
AC   A4ETV1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Beta-ketothiolase {ECO:0000313|EMBL:EBA17140.1};
GN   ORFNames=RSK20926_09222 {ECO:0000313|EMBL:EBA17140.1};
OS   Roseobacter sp. SK209-2-6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA17140.1, ECO:0000313|Proteomes:UP000005964};
RN   [1] {ECO:0000313|EMBL:EBA17140.1, ECO:0000313|Proteomes:UP000005964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA17140.1,
RC   ECO:0000313|Proteomes:UP000005964};
RA   Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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}.
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:EBA17140.1}.
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DR   EMBL; AAYC01000004; EBA17140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4ETV1; -.
DR   eggNOG; COG0183; Bacteria.
DR   Proteomes; UP000005964; 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; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
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; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005964};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          20..276
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          284..406
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        105
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        363
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        393
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   407 AA;  42442 MW;  B956426FF90CFAFD CRC64;
     MLRLHNEDNQ YMRREIMSEI VILDGARTAI GTFGGSLANT SPIDLATTAS KAAMERSGVE
     PDQIGHVVFG HVINTEPRDM YLSRVAAMQA GIPNGTPAMN VNRLCGSGAQ AIVSGIQSLM
     LGDADYALTG GAENMSKSPF IMTQQRWGAK MGDVKSLDMM LGALNCPFGT GHMGVTAENV
     ADEHEITREE MDAFALASQT RAAAAIEAGH FQSQITPVEV KVKRDMVPFE VDEHPKGTSM
     EALSGLRAVF QKDGRVTAGN ASGINDGAAA LVLARAEAAE NAGLKPKARV LGYAHAGVRP
     EVMGIGPVPA VQNLLAKTGL SASDFDVIES NEAFAAQALA VNKELGLDPT KVNPNGGAIA
     LGHPVGATGA IITLKALYEL ERTGGSKALI TMCIGGGQGI ALAIERI
//
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