ID A0A2P4UPC4_9ACTN Unreviewed; 377 AA.
AC A0A2P4UPC4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:POM26906.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:POM26906.1};
GN Name=fadA_1 {ECO:0000313|EMBL:POM26906.1};
GN ORFNames=BTM25_13140 {ECO:0000313|EMBL:POM26906.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM26906.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM26906.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM26906.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM26906.1}.
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DR EMBL; MTBP01000001; POM26906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UPC4; -.
DR Proteomes; UP000242367; 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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:POM26906.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242367};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:POM26906.1}.
FT DOMAIN 5..247
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 255..376
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 377 AA; 39839 MW; 5E91DAE480D3074B CRC64;
MAEAYIVGAV RTPVGTKKGA LKDVHPADLG AHVLKELVDR TGVDPAAVED VIMGCVMQVG
PQTLDIARTA WLSAGLPESV PGVTIDRQCG SSQQAVHFAA QGVLSGTQDL VVAAGVEQMT
KVPMGSSLVA GMEFPFGEGW GERYGQQEIT QFRGAQLMVE KWGLTREDLE KFALESHRRA
AKAIEAGYFD REIAPIAGLS KDEGARPDTT LEKMAGLNPL REGWALTAAV ASQISIGASA
LLIASEDAVR RHNLTPRARI HTLAVCGSDP VYMLTGPIPA TEKALAKSNL KIDDIDVFEV
NEAFAPVPIA WARDTGASLE KTNPNGGAIA LGHPLGATGG ILMTKMLHEL ERTGGRYGLQ
TMCEGGGQAN ATIIERV
//
