ID A0A1V2QWE7_9PSEU Unreviewed; 397 AA.
AC A0A1V2QWE7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ONI92563.1};
GN ORFNames=ALI22I_03380 {ECO:0000313|EMBL:ONI92563.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI92563.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI92563.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI92563.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:ONI92563.1}.
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DR EMBL; MTQP01000034; ONI92563.1; -; Genomic_DNA.
DR RefSeq; WP_077004079.1; NZ_MTQP01000034.1.
DR AlphaFoldDB; A0A1V2QWE7; -.
DR STRING; 1933778.ALI22I_03380; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ONI92563.1}.
FT DOMAIN 5..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..396
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 397 AA; 41260 MW; DB15C872BB2826FC CRC64;
MRDAVIVDAV RTPIGKGKPG GALSGVHPVD LHAHAIRSLV ERTGIDPSLV DDVISGAVGQ
IGEQSSNTAR WAALAAGLPE SVPGVTVDRQ CGSSQQAIHF AAQGVIAGAY DVVIASGVES
MSRVPIGSQT AGKDFLGPGV ATRYPEGLVP QGISAELIAR RWNLSRAQLD TFAAESHRRA
ATAWEEGRFT GEVAPVKATA ADGVPVHVGR DESLRSATSV DVLASLKPAF RSDTWEQRFP
QLDWKVTAGN SSPVNDGAAA LLITSSETAA RLGLRPRARL HSFAVAGDDP LYMLTGIMPA
TRKVLDRAGL ALADIDAFEV NEAFAAVVLA WQAETGADLA KVNVHGGATA IGHPLGASGA
RLMTTLLSVL EQHGGRFGLQ TMCEAGGLAN ATIIERL
//
