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Database: UniProt
Entry: D3P9J0_DEFDS
LinkDB: D3P9J0_DEFDS
Original site: D3P9J0_DEFDS 
ID   D3P9J0_DEFDS            Unreviewed;       480 AA.
AC   D3P9J0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Thiolase family protein {ECO:0000313|EMBL:BAI81380.1};
GN   OrderedLocusNames=DEFDS_1929 {ECO:0000313|EMBL:BAI81380.1};
OS   Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS   SSM1).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Deferribacteraceae; Deferribacter.
OX   NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81380.1, ECO:0000313|Proteomes:UP000001520};
RN   [1] {ECO:0000313|EMBL:BAI81380.1, ECO:0000313|Proteomes:UP000001520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC   {ECO:0000313|Proteomes:UP000001520};
RX   PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA   Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA   Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA   Takai K.;
RT   "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT   the genome sequence of the thermophilic bacterium Deferribacter
RT   desulfuricans SSM1.";
RL   DNA Res. 17:123-137(2010).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; AP011529; BAI81380.1; -; Genomic_DNA.
DR   RefSeq; WP_013008625.1; NC_013939.1.
DR   AlphaFoldDB; D3P9J0; -.
DR   STRING; 639282.DEFDS_1929; -.
DR   KEGG; ddf:DEFDS_1929; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_035425_4_0_0; -.
DR   OrthoDB; 9785768at2; -.
DR   Proteomes; UP000001520; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00829; SCP-x_thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
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   SUPFAM; SSF53901; Thiolase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001520};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          22..220
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          253..343
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   480 AA;  53463 MW;  E84A2E4220549338 CRC64;
     MGVFIYKAGL SKFGKRKSNI IHLIQEAVFN MKTDISDVDA VFIGLMNPEE FTGVGNIASY
     VLDKLGLYKI PAVRIETASS TGAAVLYYAY AAVKSGIYKN VLVIAAEKMT EMPTNRVTKI
     LAEVIHPAER KTGATMPALA ALVTNRFAYE NKIKKDVLKK LLFYVAEKNH YYGQFNEFAQ
     FRKEIDFDTY IKSKIVSSPL SLYDCAPISD GAAAVYLSSE KGDIVVAGIG QGTDRQALCE
     REIITSFEST KAAAFNAFKM AGLSPMDIDF AEIHDAFTPF EVTGLIDTGL VDKKEIIRFY
     EERLGYHDGK LPVNISGGLK SRGHPVGASG LAQVVEVYNI MNGKYNDEIS LKRCDVALTQ
     SIGGLATNNF VIILKRRGSK VKSTLRYDFN DKRKSKKEKM SKIPQIYSFT ELYITPEGVN
     SPLNLVMVQR KQKKFLARYI GDVKPKIGLK LSIKKMDNGI LYAYPEAGFI EKIRKRLKKK
//
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