ANAPS_NEOFI
ID ANAPS_NEOFI Reviewed; 2359 AA.
AC A1DN09;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Nonribosomal peptide synthetase anaPS {ECO:0000303|PubMed:19001367};
DE EC=6.3.2.- {ECO:0000269|PubMed:20225828};
DE AltName: Full=Acetylaszonalenin synthesis protein anaPS {ECO:0000303|PubMed:19001367};
GN Name=anaPS {ECO:0000303|PubMed:19001367}; ORFNames=NFIA_055290;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=19001367; DOI=10.1074/jbc.m807606200;
RA Yin W.B., Grundmann A., Cheng J., Li S.M.;
RT "Acetylaszonalenin biosynthesis in Neosartorya fischeri. Identification of
RT the biosynthetic gene cluster by genomic mining and functional proof of the
RT genes by biochemical investigation.";
RL J. Biol. Chem. 284:100-109(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=20225828; DOI=10.1021/bi100198y;
RA Ames B.D., Walsh C.T.;
RT "Anthranilate-activating modules from fungal nonribosomal peptide assembly
RT lines.";
RL Biochemistry 49:3351-3365(2010).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of the prenylated pyrroloindoline
CC diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in
CC the pathway is the formation of (R)-benzodiazepinedione by condensation
CC of tryptophan and anthranilic acid catalyzed by the non-ribosomal
CC peptide synthetase anaPS (PubMed:19001367, PubMed:20225828). The
CC prenyltransferase anaPT then converts (R)-benzodiazepinedione to
CC aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via
CC C3-prenylation (PubMed:19001367). The last step in the biosynthesis of
CC acetylaszonalenin via acetylation of aszonalenin at position N1
CC catalyzed by anaAT (PubMed:19001367). {ECO:0000269|PubMed:19001367,
CC ECO:0000269|PubMed:20225828}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:19001367}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for l- to d- amino acid conversion)
CC are present within the NRP synthetase. NRPS12 has the following
CC architecture: A-T-C-A-T-C (PubMed:19001367, PubMed:20225828). The
CC activation and loading of antranilate is performed by the first module
CC (PubMed:20225828). {ECO:0000269|PubMed:19001367,
CC ECO:0000269|PubMed:20225828}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; DS027698; EAW16180.1; -; Genomic_DNA.
DR RefSeq; XP_001258077.1; XM_001258076.1.
DR AlphaFoldDB; A1DN09; -.
DR SMR; A1DN09; -.
DR STRING; 36630.CADNFIAP00004223; -.
DR PRIDE; A1DN09; -.
DR EnsemblFungi; EAW16180; EAW16180; NFIA_055290.
DR GeneID; 4584592; -.
DR KEGG; nfi:NFIA_055290; -.
DR VEuPathDB; FungiDB:NFIA_055290; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_4_1; -.
DR OMA; ERYLEYP; -.
DR OrthoDB; 4243at2759; -.
DR BioCyc; MetaCyc:MON-18800; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Ligase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2359
FT /note="Nonribosomal peptide synthetase anaPS"
FT /id="PRO_0000438416"
FT DOMAIN 770..846
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1842..1918
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 239..633
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 883..1292
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1321..1709
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1936..2356
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT MOD_RES 807
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1879
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2359 AA; 261447 MW; 8E810B47C01FF713 CRC64;
MTITTMTPQN GTRRQVDGGP ICFFPTMTRL DMQSITFDNH VVQKLTSFPN ASDAGVHLLL
AGLWALTLRQ YAEVDTARFE VSTSILASGK GSGATKHVFS IALSPSDPVS TLFDVRNWDI
RFVDQKHSDS FNTGVFVVEN QNGRCLLDVE YHDINLLLQS NRTSAELSLV YRSSAIAGTY
ARHLADGIAQ AIISISENPN QSIGAVDFCC SLQKAQVVTW QNAKIIQPDR SFLFEYISRN
ATVHGDTLAI DSWDGQFTYA ELDGLSTVMA TRFQERGIGP GDLVPMCFGK TRWAIAAMLA
INKTGAGFVP LDPAYPQSRL ETIIQKTQAR VALASPTTES ILRPLGLPLL VISDSILGCC
LPHSKRYTAP NSGVAPAYCF FTSGSTGDPK GCEVSHLAFA SIATHARSLC LSQQSRSLQF
ASFCFGASLL EIWCTLIVGG TLCIPSDHDR LNSLGEFMAK MRINWAFITP TVLASISPDN
FNNLHLFIAG EPIGERDIRT WAPRARLFQA YGLTEWAGVF AVSRQIRTPE DRKSIGSPVN
ARAWIVDPLD HQKLAPIGAV GELVIEGPSL AQGYRGDPQR TAAVFLQRPP WLTLPALSKD
GSSSRVYKTG DLVRYAEDGS LVYVRRKDNQ VKIHGQRLEI GEVEYHVRQL FPQAKMVIVM
VHEPSDAASH QRNLVALTLH PPNNGHTGFS HGKLEFMEVD QEYQSKVEHV RNGLRSRLPA
FMIPQLFLPL SQIPTTITGK ADRRSLCRDV NKLSYAQLHG LTTQMVSTRA AQGKGEEAIH
AAVCDVLGLA PEHLGMNDNF FHLGGNSASA MKLTMSARRR GLRFTIRDVF NHPVLAELAS
AANLSNGCER PVVQTMELLE PESVSELKQL AVSQCRIDED IIEDIYPSTA LQEGLVAITA
RDPSLCKARV ICKLRSNVRI DALKAAWECV VQLNDILRTR FILSASHGTF QVVCKEPFSW
ARAQNLEDCI QQSDALVHRV GDDLVHAYII PDEKDRDSAS TFVFVAHHAL CDQWSIRLLL
DQLTAAYGHS KLPSNRFSAF IRYLTKTRSH FKNYWINQFQ GLEAVAFPPL PSPSYTPVAS
EKFDFVMKLL GNTTKQITTA TYIKLAWAVV ISCNTGSNDT VFGVTVNGRG APIDGVGELT
GPTIATIPQR IKLLPDQSAT SALAEIQSHS LEVIPYEQAG LQNIQKYSPE ARSACMFQSQ
LIIQPCPPSP PDLFEACDFS ATQTGGFSAY GLSLECQMTY DDRHCEVTAT FDPGMISRER
VQRLLQHLEL VLQDVMADPS RKVGDLPRMS RQDWDQIQRW SGTLPPVSRQ CVHDAVDERY
LEYPNACAVS APDGDLSYAE LIHSANAVAA ELLAHGVEPG KYIPVLFEKC KWSPVAMLGV
LKAGAAFVLL DPSYPPQRLH AICGGLKSQI ILCSKGLSAR AASLGPTAIA VHENATFLVD
IPNATLPVVS PEDPAYVVFT SGSTGTPKGA IIDHQSYCSS ALAHNRAHFL GRNSRVLQYA
SYAFDVSIME TLSTLMAGGC VCILSDLERH DHFADSVQRL AVTHAFLTPS TARLLMQREL
PSLCVLVMGG EVMSLADRSY WMKRVRLMNE YGIAECSVAS TIREVSDVEQ RDIGFPMGVL
AWVVDQNDHE KLVAIGAIGE LLLEGPSVGR GYLDNPEATR RAFIEQPGWL RAVRGGKTSR
VYKTGDLVQY NEDGSLSFIG RKDSQIKIRG QRFELEEVEQ HLRRIDEIKE VTAVAVAPSD
RQKQAYLVAF IVPRTRESFC VHSAKALVTH PTEEFRHLAA AIQSKLHSIL PAHMVPSIYL
PVNQMPKTSS DKVDRCRLKE EVGKWSWSDL QAYSVSSTSR RAPSNSVEQD LQRVWAQILG
IRLDSIGVED SFFHLGGDSI IAMQVVAEAR SRGLDHSVQD INQLKSIKAI ANKIGVVSTI
AQPVVQDQVT DELFGLTPIQ EFFFEKYPEG TCRFNQNILV HFQKPVADID VERAANKLVQ
NHAILRARYA RQKDGSWKQF FTGYTEQCFR FSMHKVNSVQ EMRHIIGQSQ TSLDPEHGPV
FTVDLFDHNG QQSLFMIGHH LVLDLVSWRI ILADMEAMIL DPQHQPHLTM SFQTWARLQA
EYGTRHLEPP PVQQLCSIDE PSMRKFWGAE NNANTGGDSK TRLIRVNEQL TNKLFGPSSQ
ALDVEPVELL HAAILFSFVN TFPQRPAPCI FGEAHGRETW DSSIDVTRTI GWFTTLWPVV
AQVNPSDSLE TVVRTVRQAR RAMDMHGWKH FTSIYHNTQQ TKCSAGTHLM EITFNYAGKF
QQVEQDGALF RMEPMAKQNL FDGAAELGRW AMLEINSVIL NGMLEFHVTY NRGTDEASVL
TPWMDNLVKC LEDLASGFA
