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Database: UniProt
Entry: D9XFD3_STRVT
LinkDB: D9XFD3_STRVT
Original site: D9XFD3_STRVT 
ID   D9XFD3_STRVT            Unreviewed;       406 AA.
AC   D9XFD3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Beta-ketoadipyl CoA thiolase {ECO:0000313|EMBL:EFL32636.1};
GN   ORFNames=SSQG_03154 {ECO:0000313|EMBL:EFL32636.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL32636.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) 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; GG657757; EFL32636.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XFD3; -.
DR   STRING; 591159.SSQG_03154; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_2_2_11; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          6..274
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..404
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   REGION          144..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        361
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        391
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   406 AA;  42697 MW;  BF2E2643F9BBFC1C CRC64;
     MMPEAVIVSA ARSPIGRAVK GSLKDIRPDD LAATIVQAAL AKVPELDPKD IDDLMLGCGL
     PGGEQGHNLG RIVAVQMGMD HLPGCTVTRY CSSSLQTSRM ALHAIKAGEG DVFISAGVET
     VSRYAFGSSD MPGTHNPLFA DAEARTAETA QSEGSSWHDP REDGLLPDPY ITMGQTAENL
     ARAKGVTRQD MDEFGVRSQN LAEEAIKNGF WEREITPVTL PDGTVVAKDD GPRAGVTLEA
     VQGLKPVFRP DGLVTAGNCC PLNDGAAALV VMSDTKAREL GLTPLARIVS TGVSGLSPEI
     MGLGPVEASK QALKRAGLTI DDIDLVEINE AFAAQVIPSY RDLGIPLEKL NVNGGAIAVG
     HPFGMTGARI TTTLINSLQF HDKQFGLETM CVGGGQGMAM VIERLS
//
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