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FSQF_ASPFU
ID   FSQF_ASPFU              Reviewed;        1480 AA.
AC   Q4WD47;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Nonribosomal peptide synthetase-like enzyme fsqF {ECO:0000303|PubMed:25582336};
DE            EC=6.3.2.- {ECO:0000305|PubMed:27065235};
DE   AltName: Full=Fumipyrrole biosynthesis protein E {ECO:0000303|PubMed:25582336};
DE   AltName: Full=Fumisoquins biosynthesis protein F {ECO:0000303|PubMed:27065235};
GN   Name=fsqF {ECO:0000303|PubMed:27065235};
GN   Synonyms=fmpE {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03480;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=25582336; DOI=10.1111/mmi.12926;
RA   Macheleidt J., Scherlach K., Neuwirth T., Schmidt-Heck W., Strassburger M.,
RA   Spraker J., Baccile J.A., Schroeder F.C., Keller N.P., Hertweck C.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Transcriptome analysis of cyclic AMP-dependent protein kinase A-regulated
RT   genes reveals the production of the novel natural compound fumipyrrole by
RT   Aspergillus fumigatus.";
RL   Mol. Microbiol. 96:148-162(2015).
RN   [3]
RP   FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=27065235; DOI=10.1038/nchembio.2061;
RA   Baccile J.A., Spraker J.E., Le H.H., Brandenburger E., Gomez C., Bok J.W.,
RA   Macheleidt J., Brakhage A.A., Hoffmeister D., Keller N.P., Schroeder F.C.;
RT   "Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus
RT   fumigatus.";
RL   Nat. Chem. Biol. 12:419-424(2016).
RN   [4]
RP   FUNCTION.
RX   PubMed=30194285; DOI=10.1074/jbc.ra118.004227;
RA   Lahham M., Pavkov-Keller T., Fuchs M., Niederhauser J., Chalhoub G.,
RA   Daniel B., Kroutil W., Gruber K., Macheroux P.;
RT   "Oxidative cyclization of N-methyl-dopa by a fungal flavoenzyme of the
RT   amine oxidase family.";
RL   J. Biol. Chem. 293:17021-17032(2018).
CC   -!- FUNCTION: Nonribosomal peptide synthetase-like enzyme; part of the gene
CC       cluster that mediates the biosynthesis of the isoquinoline alkaloids
CC       fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts
CC       of fumipyrrole as a shunt metabolite (PubMed:25582336,
CC       PubMed:27065235). The products of the cluster lead to a brown
CC       coloration and are important for growth and conidiation
CC       (PubMed:25582336). The nonribosomal peptide synthetase-like protein
CC       fsqF, which lacks a canonical condensation domain, is required for
CC       addition of a serine-derived dehydroalanine moiety to activated
CC       tyrosine but is not essential for the subsequent steps leading to
CC       isoquinoline formation (PubMed:27065235). A different enzyme, most
CC       likely the ATP-grasp enzyme fsqD, is responsible for activation of
CC       tyrosine (Probable). Three additional enzymes encoded by the fsq
CC       cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG
CC       and the FAD-dependent oxidase fsqB, catalyze the formation of the
CC       isoquinoline ring system in the fumisoquins (PubMed:27065235,
CC       PubMed:30194285). FsqB converts the fspF thiolation domain-bound
CC       (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-
CC       (methylamino)hexanoyl into isoquinoline (PubMed:27065235,
CC       PubMed:30194285). The cyclization most likely proceeds via a two-step
CC       mechanism, beginning with FAD-dependent oxidation of the methyl group
CC       to an iminium species followed by electrophilic attack on the
CC       deprotonated phenol (Probable). {ECO:0000269|PubMed:25582336,
CC       ECO:0000269|PubMed:27065235, ECO:0000269|PubMed:30194285,
CC       ECO:0000305|PubMed:27065235}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- INDUCTION: Expression is positively regulated by the fumisoquins
CC       biosynthesis specific transcription factor fsqA (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336, ECO:0000269|PubMed:27065235}.
CC   -!- DOMAIN: FsqF lacks the condensation domain that is essential for
CC       canonical peptide bond formation, and bioinformatic analysis of the
CC       vicinity of fsqF did not reveal any genes that could code for a second
CC       NRPS or free-standing condensation domain.
CC       {ECO:0000305|PubMed:27065235}.
CC   -!- DISRUPTION PHENOTYPE: Prevents the production of fumipyrrole and leads
CC       to reduced growth and sporulation, but does not affect virulence in
CC       infected mice (PubMed:25582336). Abolishes completely the production of
CC       isoquinolines as well as of pyrroles and leads to the production of a
CC       single brightly red shunt metabolite, the anthranilic acid-substituted
CC       isoquinoline (PubMed:27065235). {ECO:0000269|PubMed:25582336,
CC       ECO:0000269|PubMed:27065235}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; AAHF01000012; EAL85691.1; -; Genomic_DNA.
DR   RefSeq; XP_747729.1; XM_742636.1.
DR   AlphaFoldDB; Q4WD47; -.
DR   SMR; Q4WD47; -.
DR   STRING; 746128.CADAFUBP00009215; -.
DR   EnsemblFungi; EAL85691; EAL85691; AFUA_6G03480.
DR   GeneID; 3505176; -.
DR   KEGG; afm:AFUA_6G03480; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1549; Eukaryota.
DR   HOGENOM; CLU_000022_60_8_1; -.
DR   InParanoid; Q4WD47; -.
DR   OMA; ADSWLFI; -.
DR   OrthoDB; 58997at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P: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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR01746; Thioester-redct; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1480
FT                   /note="Nonribosomal peptide synthetase-like enzyme fsqF"
FT                   /id="PRO_0000438873"
FT   DOMAIN          662..741
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          31..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..527
FT                   /note="Adenylation domain"
FT                   /evidence="ECO:0000255"
FT   REGION          739..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..1003
FT                   /note="NAD-binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1100..1465
FT                   /note="Aminotransferase domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         700
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1480 AA;  163306 MW;  45137566A9EAC7BE CRC64;
     MLLQDVHHRE QLDDDVENAF SKINGTARQA SPFADEPSID VPSTHLPVVT PRSKTANDRT
     GLAKSLPYAS LGASRSTIDE QDVLIQTWAI LLHQYAVSDT VAFAIIGKSD PSGYSGRRAS
     TQVVCLPHLF LDSARATPHA PAVHGWDGRL TYAELDQLSN SVARQLLRRG VRKGQFVPFS
     FEKSIWMVVA IIGILRAGGV VASIDPSQPQ SRAREIIQET GATVIVASTA QASVFAGLVD
     TVVPIADDTV HPAANDTGLH PSLPPVHPED PAVVIFTSGS TGKPKGIVIQ HGAVTTRMVA
     EGRAFQYHGA RTLQFAASTW DIFMTDIFTT LAFNGCVCIP SEEDRRFNLA RFCAEYDVSL
     ALITPSLANL LEPTGFPTLK TLIFGGEALK EEVTRKWEAV DGISLHQGYG PAETGPCVAG
     RLAERPEILG YALDNSVCVL VDPSNPNRLV PLGAVGELVV GGPSLLREYI NDPRKTEAAV
     IENPPWALDL MTPVRRFYRT GDLLRYSVDT LDGRLEFVGR TDDQVKYHGQ RIELGEIEHH
     LSRLPGVEAC VVVLAKAGFF KDRLVAVVQA GKSSGGSSYG TQLSLRSDPN ITITHMRRFL
     SSRLPEFMIP NELLVVQELP HNNSMKLDRG RVAKWVADMQ SQPSEAVPKP HTRGNELLAH
     ESTARTIARE YARIVAGDSV ARRREYEDRD FNLQEGGIDS IQIMSLSMFL TEHFGFQVPM
     ADILSSRATV RSIASLIDAN SSPGRGQPLN TQETARLPLR SNGPAPSQQA LERNGSRVFL
     TGASGFLGIE ILRQLLARPK THVYALVRGS SESQARERLV QKAISAGWWQ DAYRTRLHVW
     HGDLTQPQLG LSQLQWQMLQ GKASPSIDAI IHNGAKVHYS QDYETLKKTN VSPTVELLKA
     VHDREEPLHS FVFVSGGQQL SFDDREDEKN AAKSLKGSGY ARSKAVSEQI VRRFANQKGS
     KARHVRIVKP GFIIGDAERG LANQSDFIWR LIAACVELGF YNGDEADSWL FISDITRVAQ
     VILHSVFEDD SQPVTKVLDG LRFKTLWALL QDKFGFELQP LSRREWLARL KHSVATKKEK
     HVLLREQFPA LHHGVVPFNN AAGTVVHREA AESTHRYMTS FPYELGRDDP ASAAKTQRLQ
     DRFAELAAFM NADPDEIAFG QSTTFLLRSL GQALKPLLNS DCEIIVSILC HEGSAAAWVA
     LAKDLGIAIK WWAPPPGDDP VLSLDTLRPL LTPKTRLVAC NHVSNVVGTI HPIRQVADLV
     HRIPGAVLVV DGVAWAPHRP IDVKALDVDF YCFSWYKVFG PHVAQLYGRR SAQKRALAGI
     SHFFLSEMPG LDWRLRLGAN SFELEEALVP ITRYLKRVGW DNIIAQETVL QDVFLAYLRR
     RPRVFRIFGE QSSDPAKRVP VITFEVIGHS STVVANKVNQ RGRFRVVSGN CWAPRPTHDV
     LGLGADGLIR VSFVHYNTVA EVQEFCTELD SVLETLNAGI
 
 
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