ID IMQB_ASPFN Reviewed; 3332 AA.
AC B8NI19;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Nonribosomal peptide synthetase imqB {ECO:0000303|PubMed:29182847};
DE Short=NRPS imqB {ECO:0000303|PubMed:29182847};
DE EC=6.3.2.- {ECO:0000305|PubMed:29182847};
DE AltName: Full=Imizoquin biosynthesis cluster protein B {ECO:0000303|PubMed:29182847};
GN Name=imqB {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064240;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP INDUCTION, FUNCTION, DOMAIN, AND PATHWAY.
RX PubMed=29182847; DOI=10.1021/acschembio.7b00731;
RA Khalid S., Baccile J.A., Spraker J.E., Tannous J., Imran M.,
RA Schroeder F.C., Keller N.P.;
RT "NRPS-derived isoquinolines and lipopetides mediate antagonism between
RT plant pathogenic fungi and bacteria.";
RL ACS Chem. Biol. 13:171-179(2018).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of imizoquins A to D, tripeptide-derived
CC alkaloids that serve a protective role against oxidative stress that
CC are essential for normal germination (PubMed:29182847). ImqB is a
CC canonical three-module NRPS that assembles the tripeptide backbone of
CC the imizoquins via condensation of Trp, Tyr, and Leu-derived precursors
CC (PubMed:29182847). N-methylation by imqF and phenol oxidation by imqC,
CC followed by cyclization via the FAD-dependent oxidase imqH carry out
CC the three-step transformation of L-tyrosine into tetrahydroisoquinoline
CC (PubMed:29182847). Importantly, this sequence requires the presence of
CC a free amine in the tyrosine moiety, indicating that isoquinoline
CC formation occurs prior to peptide bond formation (PubMed:29182847). The
CC imidazolidin-4-one ring of imizoquins could form following additional
CC oxidation of the methyl-derived bridgehead carbon by imqH
CC (PubMed:29182847). Lastly, O-methylation by imqG and leucine
CC hydroxylation by imqE complete biosynthesis of the imizoquins
CC (PubMed:29182847). {ECO:0000269|PubMed:29182847}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29182847}.
CC -!- INDUCTION: Expression is down-regulated by ralstonins, lipopeptides
CC produced by the plant pathogenic bacteria Ralstonia solanacearum
CC (PubMed:29182847). Expression is positively regulated by the imizoquins
CC cluster-specific transcription regulator imqK (PubMed:29182847).
CC {ECO:0000269|PubMed:29182847}.
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, epimerase (E) domains
CC (responsible for L- to D-amino acid conversion) are present within the
CC NRP synthetase (By similarity). ImqB has the following architecture: A-
CC T-C-A-T-C-A-T-TE (PubMed:29182847). {ECO:0000250|UniProtKB:Q4WAZ9,
CC ECO:0000305|PubMed:29182847}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED49603.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963479; EED49603.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002379984.1; XM_002379943.1.
DR SMR; B8NI19; -.
DR STRING; 332952.B8NI19; -.
DR ESTHER; aspfn-imqb; Thioesterase.
DR EnsemblFungi; EED49603; EED49603; AFLA_064240.
DR VEuPathDB; FungiDB:AFLA_008358; -.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_0_12_1; -.
DR Proteomes; UP000001875; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 3.
DR CDD; cd19545; FUM14_C_NRPS-like; 2.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
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_com.
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 InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 3.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..3332
FT /note="Nonribosomal peptide synthetase imqB"
FT /id="PRO_0000444550"
FT DOMAIN 764..846
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29182847"
FT DOMAIN 1880..1954
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29182847"
FT DOMAIN 2963..3039
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:29182847"
FT REGION 230..622
FT /note="Adenylation 1"
FT /evidence="ECO:0000305|PubMed:29182847"
FT REGION 886..1314
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29182847"
FT REGION 1336..1740
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29182847"
FT REGION 1992..2402
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29182847"
FT REGION 2422..2819
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29182847"
FT REGION 3058..3323
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:29182847"
FT MOD_RES 801
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1915
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3000
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3332 AA; 367538 MW; 77D3876E57D65A9C CRC64;
MLSPAVCYHT DEGKNGYTFP NLETPKNGVV QTPVQYLIQT APLHDFCSHQ MVDLRTLLQC
AWSRVIAQLD STTDLKADAI YGTKSKSLLE GFISEVKKSQ QSTQLENERI LTEKLLLPLN
PRGTSSLSWL QNDLLCATGG EYGEQSTGGF ELAQCGSWIA ISASFNPLIV SSRWVNDYIE
VFRSFLVALV VGDDELSAPE NYLTPEDCAR IRNWNSAVPP EINASILDVF SEQVKAHPGS
TAVSGWDASL TYQELEDCAD QLAYQLQSRG VGPGMLIPLC FEKSAWTVVA IIAVISTGAA
FVLLDASQPE ARLRSIVMQT RATLMITSSQ KKDLGRRLVP EVVSVQPTKS TKNSERSRAL
RPVIKPDSLL YVVFTSGSTG QPKGAMISHS NFVSAVHYRR SELYNVTPRV LDFASYSFDI
SIESTLAPLL LGGCVCVPSD ASREADPSDA IKAFNVNQVM LTPSVARLVE PENVPSLRLL
HLGGEQISRF DIERWPSTVK LINGYGPAEC TVVSTANTVS PSSPEAHTIG RGLGAVTWVV
DPADTGRLVP VGAVGELVIE GPLVGSGYLH DEGRTLAAFI VDPPWLRAFG RRGRLYRTGD
LVSYNSNGTL TFIGRKDTQV KVNGQRVELG EIEHNLQQEI YNQGNCVVDV VVDLISVNSN
SGKQSILLAF LGLERAAQER FAASGTPSVQ ELTSAMWEIL EPINLFKVLP RYMVPSIYIP
LWRMPLLPSG KINRLKLRSM GESLSVDDLA AFRKPQVATV DTQGRITPQE KLLQSLWGQI
FPHCAGSIQP DDNFFSLGGD SLTAMKLVGL IRKHGIENKH SETIRIADIL QWPRLADMAR
CITRVDDKQG DVQDALFDLL PDHIAPSNAR QIAAPQCDVQ PEQIVDIYPC TPLQEGLMAL
SAERSGAYIA QNIFELSDRT NIDTLRMAWT HIVMSSVIFR TRIVQLDSQT LAQAVVTVPI
EWECYDGKLN DFVAIDRHRP MGIGKALMRL TVVTERSEES LLKCFLVWTA HHAVFDDWIL
NLITSLVGKM YHGRPPSSFH LTPYKRFIRH LQELNRESFS NYWRQELEGT NAAIFPHLPS
AVDKPVADAT ANFAFSLNDS KLNVHASLPT ILRAAWSILV SRHTQTDDVI FGETLTGRNA
PVAGVEEMDG PTLTTIPRRV KVQNEMRVAE FLEEIRRHEI NSIPYEGFGL QNIQKLSDDA
RTACQFATLL VIQRDPEVSF DSPMINVTEK VLHEDCGEDG KPYASFFTTY PLMVTISIKD
NQINIYASFD SRIIERSQMQ VLMHQLEVIT RQVIQEPHEV VGGINCLTRK ELHQIWSWNR
LPWVPVSGSV HDSIAEVSNT RPTAPAVCAW DGSLTYGELD NLSTRLGSYL FKVGVEAESL
VPLCFEKSVW TIVSMLAVIK AGGAFVLLDP TQPKQRLGEI IVRAKANYVL TSPLQYGMVS
DLASEFNLTI VLVSKSPLDA LTDDATVTDR MPQHLDSDRP LFVTFTSGST GKPKGVISTH
GSYLSGVNYR RSILQLPNLD MRVFDFASYS FDVSTDVILS TLLTGGCVCV PSDFDRKNNI
PGAINALRVN AADLTPSVSR LLSPESVPGL KVLKLGGEAN TAADHALWLG KTTLVNIYGP
SECLVVTAKT VLPGIDPCNI GRGLGANTWV ADPTNHDRLA PIGSIGELLV EGPILGRGYL
DDQKQTDAVF IHNPTWLVKG LPGFQPGREG RVYKTGDLVR YNPDGTLHYI GRKDRQLKVR
GQRVEPAEIE GAIKRHMQSK LGMTIDVVAD LVTSNRDQRK RLIAFLGLNQ VLESRGYSEK
DHLGDTVLRD IMWEVTAGLE VLLSQTLPPY MVPSVYVPLR HIPLLPSGKT DRRKLQSAAA
SLSPEDLSFF RERPKAQNRA IATPKEEKLQ KIWADALGVK SIQAEDNFFT IGGDSIAAMR
LVGLARDQGL LLSVADIFQR PRLYEMAEKA AETGTELLDI PAFSLLPGAN PYVIDEREVA
AAQCGCSIEL IEDIYPCTPL QEGLMALSTK TPGAYISQNV FQMGNATNTD LMKEAWDYVV
RSNPIMRTRV ILSARQDLVQ VTVQEGIHWA SHDSLDCYLK YDRNTSMGLG MPLTRLAWVD
DEMTKRSFLV WTAHHAIFDG WVLSLVMENV IRVYHGKSLH VGPPFKAFIK YLKELERAQM
DTFWQDEFSG ITATPFPALP SSTYQPKADV ETKLEMSFTW STTSNVTSST FLRLAWAVLV
ARLTASSDVI FGETLNGRNA PIPGIERMIG PTLTTLPRRI VLEDGLPVAD LLHRLKDHEI
AMMPFEHVGL QHLQELSADC QAACKFQTLF VVQRGMDHDM SEMSLTISGD VSNFNSYALM
LTCAPESDKI LFHASHDSNV ISPEKMQDVL NQLQNVVMQL SKKMDRPLRE INCLSEIDTQ
QIWKWNHQLP ESISIPVHEI IAQQAREHPA TEAVCAWDGT FTYRELDTLA GQLAYHLKEL
GAVSTPGYHI PLCFEKSAWT VISILAVMKA GGSFVLLDVS QPQDRLQHIV SHIKANYILS
SPRQSDLASS LAANVVVVSS DFVRSLRQLH TPGPLNPNSA LYVVFTSGST GKPKGVIITH
LNFASGVHYR QNVMHMPGFR LLDFPSYSFD ASVESNLVPL MIGGCVCIAS DELCQNNLSA
AISSTNANAV MLTPSSATLI SPENAHSLKQ LHLGGEKLTA ANIETWADKL KLVVGYGPAE
CAVTTTGRIV KGMVPQKENI GPAFGAVTWL VDPASHDRLV PLGTIGELLI EGPIVGQGYV
NDPERTAAAF IENPPWLLAG GGMFAGRQGR LYKTGDLARY DSDGTLIFIG RKDTQVKIRG
QRVELQEIEH HVYQYLRDLT GLGLSIVADL ISTCSDIANP TLVVFIELEA VMTQKGYLPD
PGPAVLYNEM KSMVPGLDEA LRNALPRYMI PSAYVPRWKL PMMPSGKLNR KQLRSDAESL
TAEQWNHFRS LISAVSPAAR GREVATNDEA AVQRLWADIL RIAEKQIKAD DSFFTLGGNS
ITAMKLVELA RRRGILFNVA DVFAHPVLSD LASRIGRVET TPLNQDDLAY APLQRLMSSN
PTLIQGQSSN IPLVMIHDGG GTTYAYHRMG PVNRPLYGIH FPGYASGTAW KGGIKSLGRH
YADLIQKSLL SGPIILGGWS SGGLISLEVA LCLKSGPFEV KGVIMVDSVF PAPSLVDETF
LAPSSSETND TAMAADGTLA KMNMFQFNSM LKEYSPPRFE DLFQDLDASK AGLCHEQRSN
VNPITEDTHH AERFPVHLLR ASSTKASIGE LDENMKSFLD ATLGWEHYRP RLVSEVDLID
AEHYSLFSAN TVAETTRHIR DFCDRITKSR KV
//
