ATRA_ASPTN
ID ATRA_ASPTN Reviewed; 920 AA.
AC Q0CT94; A0A2I6SS17;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Nonribosomal peptide synthetase atrA {ECO:0000303|PubMed:29305695};
DE EC=2.3.1.- {ECO:0000269|PubMed:29305695};
DE AltName: Full=Atromentin synthetase {ECO:0000303|PubMed:29305695};
GN Name=atrA {ECO:0000303|PubMed:29305695}; ORFNames=ATEG_03090;
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 [MRNA], DOMAIN, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=NIH 2624 / FGSC A1156;
RX PubMed=29305695; DOI=10.1007/s00253-017-8719-1;
RA Huehner E., Backhaus K., Kraut R., Li S.M.;
RT "Production of alpha-keto carboxylic acid dimers in yeast by overexpression
RT of NRPS-like genes from Aspergillus terreus.";
RL Appl. Microbiol. Biotechnol. 102:1663-1672(2018).
RN [2]
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.
CC -!- FUNCTION: Nonribosomal peptide synthetase that mediates the
CC biosynthesis of atromentin (PubMed:29305695). AtrA first activates 4-
CC hydroxyphenylpyruvate (HPPA) through its A domain to AMP-HPPA
CC (PubMed:29305695). The HPPA unit is then loaded to the T domain and
CC eventually transferred to the TE domain (PubMed:29305695). Another HPPA
CC unit is then loaded onto the T domain (PubMed:29305695). The TE domain
CC then catalyzes the condensation of the two HPPA units and the release
CC of atromentin via cyclization (PubMed:29305695).
CC {ECO:0000269|PubMed:29305695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 3-(4-hydroxyphenyl)pyruvate + H(+) = atromentin + 2 H2O;
CC Xref=Rhea:RHEA:63968, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:149642;
CC Evidence={ECO:0000269|PubMed:29305695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63969;
CC Evidence={ECO:0000269|PubMed:29305695};
CC -!- DOMAIN: AtrA 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:29305695}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU36364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; MG384315; AUO29225.1; -; mRNA.
DR EMBL; CH476597; EAU36364.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001212268.1; XM_001212268.1.
DR AlphaFoldDB; Q0CT94; -.
DR SMR; Q0CT94; -.
DR STRING; 33178.CADATEAP00008280; -.
DR EnsemblFungi; EAU36364; EAU36364; ATEG_03090.
DR GeneID; 4317854; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_337691_0_0_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 1: Evidence at protein level;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..920
FT /note="Nonribosomal peptide synthetase atrA"
FT /id="PRO_0000450546"
FT DOMAIN 558..637
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 13..428
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29305695"
FT REGION 656..905
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29305695"
FT MOD_RES 595
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 920 AA; 101892 MW; 62971A07F4493E3A CRC64;
MSFKNLQQLL KEAAAQERCG RVICYSSGNL QNPTSRSYHE LMQEAQRASW ALRTATCARH
GSAVLLHFDS HWDSILWFWA TLLAGCVPVM STALPNNTSL RTAHLEHLSR TLNGPLCLTR
ARMAPEFSEQ TCIEPIAVET FDMQTSSKED HVDSAPDDTA VMMLTSGSTG RPKAVCLTHG
QILSSIVNKL SVVPLRGPFM NWIRLDHVAA LTEIHLPAIL SNKDQVHVQS ADLLANPVEF
IRLASEHRVA KTFAPNFFLA TLRDALCATQ HDSPKWDLSG LYIFSGGEGN VTRTCDEISK
LLGRYGAPPN VIVPGFGMTE TCAGAINNTS CPWYDIERTS DFASLGTCMS CIRMRITDDS
GGNTCVSPGE TGNLEVTGSA VFKEYFNNPS ATADAFTSDG WFKTGDRGLI DTNGYLHLAG
RLKETMIING VKYSPHEIES VLDESNIPGL TPSYNCCFCS FPPGAETEVI CLVYLPTYPE
EDIRARIQTT DAISKCIVML TGSRPVIIPL DKGLLQKSAL GKLSRSSIKA SYEKGEYKAY
QDTNSHLVKM YRQAMRTPPK DELERSLLAI FVDSLELSEE EFDVQTPVFD LGITSIDLIR
LKKSIEEQRD IDQEIPMTTL MANTTVRELS AALHDLQAPG TYKPVITLQN EGSKTPLWLI
HPGVGEVLVF LNLAKYIKDR PVYALRARGF GAHETPFASI EETVRTYYAA IKAKQPRGPY
AVAGYSYGTM LAFEVSKQLE QGGDTVGFVG SFNLPPHIKT RMRQLDFTEC LLHLAYFLAL
MSEQRAGELA AAFAGVQPSQ ERVLDEVMQN ADPVRLAELQ LSRQYLLQWA NLAFALQSMA
VDYDPSGSVA RMDVFYCVPL AVAAASKQRW REEHLSQWRD FTRSEPRFHD VGGAHYTMLA
PEHVFGFQKT LRGALEARGI
