PNGA_ASPTN
ID PNGA_ASPTN Reviewed; 946 AA.
AC Q0CBN5; A0A2I6SS13;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Nonribosomal peptide synthetase pngA {ECO:0000303|PubMed:26851300};
DE EC=6.3.2.- {ECO:0000269|PubMed:26851300, ECO:0000269|PubMed:29305695};
DE AltName: Full=Phenguignardic acid synthase {ECO:0000303|PubMed:26851300};
GN Name=pngA {ECO:0000303|PubMed:26851300}; ORFNames=ATEG_08899;
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.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=26851300; DOI=10.1016/j.fgb.2016.01.014;
RA Sun W.W., Guo C.J., Wang C.C.;
RT "Characterization of the product of a nonribosomal peptide synthetase-like
RT (NRPS-like) gene using the doxycycline dependent Tet-on system in
RT Aspergillus terreus.";
RL Fungal Genet. Biol. 89:84-88(2016).
CC -!- FUNCTION: Nonribosomal peptide synthetase that mediates the
CC biosynthesis of phenguignardic acid (PubMed:26851300, PubMed:29305695).
CC PngA alone is sufficient for phenguignardic acid synthesis
CC (PubMed:26851300, PubMed:29305695). PngA first activates phenylpyruvic
CC acid (PPA) through its A domain to AMP-PPA (PubMed:26851300,
CC PubMed:29305695). The PPA unit is then loaded to the T domain and
CC eventually transferred to the TE domain (PubMed:26851300,
CC PubMed:29305695). Another PPA unit is then loaded onto the T domain
CC (PubMed:26851300, PubMed:29305695). The TE domain likely promotes the
CC enolate formation on the attached unit, followed by a nucleophilic
CC attack on the carbonyl to yield an ether linkage between the two units
CC (PubMed:26851300, PubMed:29305695). Finally, the TE domain probably
CC catalyzes a similar reaction to give the cyclized dioxolanone core and
CC releases phenguignardic acid (PubMed:26851300, PubMed:29305695).
CC {ECO:0000269|PubMed:26851300, ECO:0000269|PubMed:29305695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 3-phenylpyruvate + H(+) = H2O + phenguignardate;
CC Xref=Rhea:RHEA:63904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:149629;
CC Evidence={ECO:0000269|PubMed:26851300, ECO:0000269|PubMed:29305695};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63905;
CC Evidence={ECO:0000269|PubMed:26851300, ECO:0000269|PubMed:29305695};
CC -!- DOMAIN: AtrA has a 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:26851300, ECO:0000305|PubMed:29305695}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU31031.1; Type=Erroneous gene model prediction; Evidence={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; MG384316; AUO29226.1; -; mRNA.
DR EMBL; CH476606; EAU31031.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001217485.1; XM_001217484.1.
DR AlphaFoldDB; Q0CBN5; -.
DR SMR; Q0CBN5; -.
DR STRING; 33178.CADATEAP00006426; -.
DR EnsemblFungi; EAU31031; EAU31031; ATEG_08899.
DR GeneID; 4323094; -.
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:0016874; F:ligase 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; 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; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..946
FT /note="Nonribosomal peptide synthetase pngA"
FT /id="PRO_0000438985"
FT DOMAIN 580..659
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 32..450
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26851300"
FT REGION 681..933
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26851300"
FT MOD_RES 618
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 946 AA; 104487 MW; 3CC586663048BA9F CRC64;
MNKKLKLFSM PGAQTSQIVI MLFQSLLHLL EAIASREPTR YIITYSIGNT HTPEIFSYSD
LLQSARKAAG ALRFKYHVVP GSVVLLHFND HWNSMLWFWA TLIADCIPAM STPFSNNPET
RLRHLKHLST TLRSPKCLTT ASLAAEFAGQ EYITPICVQS LDYENLVHLP IKEGGDIAVL
MFTSGSSGHC KVVPLTHEQI LASLSGKAWT FPLPDNTAQL NWVGMNHVAS LVEVHLFSIY
THSDQVHIPT VEVLSHVTLF LDLIHRHRVS RTFAPNFFLA KLRAALSADD TLAKYTGSLS
NLRYIVSGGE ANVTQTINDL AQMLKKCGAV SNVIVPAFGM TETCAGAIYN TSFPQYDVEH
GLPFASVGSC MPGIQVRIVQ LNGNGNSVPP GTVGNLEICG PVVLKGYFND PAATKSTFTN
DNWFKTGDLA FVDDNGMLVL AGREKDSIIV NGANYSPHDI ESAIDEANIP GLISGFTCCF
STFPPSADTE EVIIVYLPNY TPADTVRRSE TAAAIRKVAM MSVGVRATVL PLDRTMLEKS
TLGKLARGKI KAAYERGDYK SYQEANEQMM ALHHKVSHHQ PRSGLEQSLL GVFTRTIPEN
LTEDFDVLTS IFDLGITSIE LLKLKRGIED LIGHGQIPLI TLMTNPTIRT LSDALKQHAQ
QRDCSIYNPV VVLQSQGKKP PIWLVHPVGG EVMIFMNLAK FIIDRPVYGL RARGFNDGED
PFHTFEEIVS TYHASIKEKQ PSGPYAIAGY SYGAKVAFDI AKALEHNGDE VRFLGLLDLP
PSLNGTQMRA VAWKEMLLHI CRMVGVIREE GIKKIYPRLE PENISPRHAI ETVMGEADVT
RLAELGLTAS ALERWANLTH ALQRCIVDHK TNGSVAGADA FYCDPMASMA ISNEQWACDY
IGKWSDHTRS PPRFHHIAGT HYTILDAENI FSFQKTFLRA LNDRGI
