ID K4R0A4_STRDJ Unreviewed; 404 AA.
AC K4R0A4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:CCK26069.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:CCK26069.1};
GN Name=fadA1 {ECO:0000313|EMBL:CCK26069.1};
GN ORFNames=BN159_1690 {ECO:0000313|EMBL:CCK26069.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK26069.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK26069.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4913 {ECO:0000313|EMBL:CCK26069.1};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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; HE971709; CCK26069.1; -; Genomic_DNA.
DR RefSeq; WP_015656464.1; NC_020504.1.
DR AlphaFoldDB; K4R0A4; -.
DR STRING; 1214101.BN159_1690; -.
DR KEGG; sdv:BN159_1690; -.
DR PATRIC; fig|1214101.3.peg.1714; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_11; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000008043; Chromosome.
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; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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 ECO:0000313|EMBL:CCK26069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CCK26069.1}.
FT DOMAIN 6..230
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 282..403
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 93
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 360
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 390
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 404 AA; 42190 MW; F21312247EC26B17 CRC64;
MSTEAYVYDA IRTPRGRGKA NGALHGTKPI DLVVGLIHEI QARRPGLDPA AIDDIVLGVV
GPVGDQGSVI ARIAAIAAGL PDTVAGVQEN RFCASGLEAV NLAAMKVRSG WEDLVLAGGV
ESMSRVPMAS DGGAWFNDPM TNLDVNFVPQ GIGADLIATI EGFSRRDVDE YAALSQERAA
TAWKEGRFEK SVVPVKDRSG LVVLDHDEHL RPGTTADSLG KLKPSFADIG DLGGFDAVAL
QKYHWVEKID HVHHAGNSSG IVDGASLVAI GSKAVGERYG LTPRARIVSA AVSGSEPTIM
LTGPAPATRK ALAKAGLTID DIDLVEINEA FAAVVLRFVR DMGLSLDKVN VNGGAIALGH
PLGATGAMIL GTLVDELERQ DKRYGLATLC VGGGMGIATI VERV
//
