ID   ATQA_ASPTN              Reviewed;         962 AA.
AC   Q0D034;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Nonribosomal peptide synthetase atqA {ECO:0000303|PubMed:23841722};
DE            EC=2.3.1.- {ECO:0000305|PubMed:23841722};
DE   AltName: Full=Didemethylasterriquinone synthetase {ECO:0000303|PubMed:23841722};
GN   Name=atqA {ECO:0000303|PubMed:23841722}; ORFNames=ATEG_00700;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=23841722; DOI=10.1021/ol401384v;
RA   Guo C.J., Knox B.P., Sanchez J.F., Chiang Y.M., Bruno K.S., Wang C.C.;
RT   "Application of an efficient gene targeting system linking secondary
RT   metabolites to their biosynthetic genes in Aspergillus terreus.";
RL   Org. Lett. 15:3562-3565(2013).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of asterriquinone CT5, a natural product
CC       that displays potential biological activities including antitumor and
CC       insulin mimic activities (PubMed:23841722). The nonribosomal peptide
CC       synthetase atqA is responsible for the production of the benzoquinone
CC       derivative didemethylasterriquinone D (DDAQ D), via condensation of 2
CC       indole pyruvic acid (IPA) molecules (PubMed:23841722). The symmetric
CC       connectivity of the 2 IPA molecules is thought to arise by head-to-tail
CC       dual Claisen condensations catalyzed by the TE domain of atqA (By
CC       similarity). DDAQ D represents the core structure of asterriquinones
CC       and is further modified by yet unidentified tailoring enzymes to lead
CC       to the production of asterriquinone CT5 (PubMed:23841722).
CC       {ECO:0000250|UniProtKB:A7XRY0, ECO:0000269|PubMed:23841722}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:23841722}.
CC   -!- DOMAIN: AtqA has an A-T-TE domain architecture (Probable). The
CC       adenylation (A) domain recognizes and activates the aryl acid
CC       substrates, and loads them onto the thiolation (T) domain (Probable).
CC       The thioesterase (TE) domain shares the missing condensation (C) domain
CC       function, and is responsible for condensation and final product release
CC       (Probable). {ECO:0000305|PubMed:23841722}.
CC   -!- DISRUPTION PHENOTYPE: Abbolishes the production of asterriquinone CT5.
CC       {ECO:0000269|PubMed:23841722}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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; CH476594; EAU39346.1; -; Genomic_DNA.
DR   RefSeq; XP_001210786.1; XM_001210786.1.
DR   AlphaFoldDB; Q0D034; -.
DR   SMR; Q0D034; -.
DR   STRING; 33178.CADATEAP00005778; -.
DR   EnsemblFungi; EAU39346; EAU39346; ATEG_00700.
DR   GeneID; 4355455; -.
DR   VEuPathDB; FungiDB:ATEG_00700; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_23_6_1; -.
DR   OrthoDB; 127131at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..962
FT                   /note="Nonribosomal peptide synthetase atqA"
FT                   /id="PRO_0000450545"
FT   DOMAIN          595..672
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:23841722"
FT   REGION          34..462
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23841722"
FT   REGION          694..951
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:23841722"
FT   MOD_RES         630
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   962 AA;  106210 MW;  E1AFE0158B05E8E8 CRC64;
     MTRTEILSNG HAEPASNGMV QYPFDNVVDA LRAAANTTEG IIAYQTNNSG SETTPAQHIS
     YKELLRTAEA NAALLQSKHL TTPKQPVVVH SDNAVDSMIW YWSVLLTGAI PTMTGPGMFS
     QDAVERKKHL LHLHRTLDAP LCLTRRALMG PFNENAGLLQ CLAFEDLSPS PDGSNASLPP
     SINPSPMDVA ALMLTSGSSG TAKAVPITHQ QVLAALRGKT AVAQLSHPTS PFLSWVHMDH
     VANLVHCHLF AIVAGVSQVQ VPAANVLVDP MQLLNLLSRH RVSRTFAPNF LFAKLRRQFD
     AGRTDSLDAD LNLAALYLDT GGEANVIDVC AGLQPILARY GAPADVFKPS FGMTETCAGC
     IFNSHCPSYD QARLHEFASL GTPMPGVRMR ISRLDGSGEA APGERGHLEI TGEAIFHGYY
     NNPTATADAF TADGWFRTGD LAYIDAGGHL HLDGRTKEMV NINGVKYLPH ELDAALEQAE
     IPGATPTYFC CFGTRTAAMD TEVVAVLYLP AYDEADDAAR FDAQSSIIRL ISMYTHSRPR
     VVPLRREDMP KTTLGKLSRA KLQAALEAGQ FAAYEAANEA AIRRHRDTMR GEPASAEEAT
     ILSIIREQLE IPEADDFGVT DSILSMGATS MDLVAIMQRV NRQLQLRKTL ALTDMLNYAT
     ARGLCQRIAA TSGTGRKHVY DPVVVLQPHG RKTPLWLVHP GVGEVLVFVN LAHHITDRPV
     YAFRAKGFNA AEGETPFTSL EEVFETYKAA MKARQPQGPY AIAGYSFGGM VAFEIAKRLE
     AEGDEVRYCG SWNLPPHIKW RMKQLLWDEC IIHLFYFVDL MDEETAYTHK PKLCELERQG
     RRLEAVRYLR QHSNPARWDE LGLSEEYYLL WVNLASNMQG MATEYEPSGN VKHLDVFVAD
     PLTHVARTRE EWVNGLLAAW KDFVREGVRY HHVEGAHYTM LKPEYVANFA KTLRTVLRER
     GV