ID   MICA_EMENI              Reviewed;         938 AA.
AC   Q5B7T4; C8VHM5;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Microperfuranone synthase {ECO:0000303|PubMed:22627757};
DE            EC=2.3.1.- {ECO:0000269|PubMed:22627757};
DE   AltName: Full=Nonribosomal peptide synthase micA {ECO:0000305};
GN   Name=micA {ECO:0000303|PubMed:22627757}; ORFNames=AN3396;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=22627757; DOI=10.1007/s00253-012-4098-9;
RA   Yeh H.H., Chiang Y.M., Entwistle R., Ahuja M., Lee K.H., Bruno K.S.,
RA   Wu T.K., Oakley B.R., Wang C.C.;
RT   "Molecular genetic analysis reveals that a nonribosomal peptide synthetase-
RT   like (NRPS-like) gene in Aspergillus nidulans is responsible for
RT   microperfuranone biosynthesis.";
RL   Appl. Microbiol. Biotechnol. 96:739-748(2012).
CC   -!- FUNCTION: Microperfuranone synthase is the only protein required for
CC       the biosynthesis of the secondary metabolite microperfuranone from
CC       phenylpyruvic acid (PPA) (PubMed:22627757). Several steps for the
CC       microperfuranione biosynthesis have been proposed (PubMed:22627757).
CC       These steps include the activation of PPA, by the micA adenylation (A)
CC       domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to
CC       the thiolation and peptide carrier (T) domain and eventually
CC       transferring to the thioesterase (TE) domain (PubMed:22627757). After
CC       loading another PPA unit onto the T domain, aldol condensation
CC       establishes the carbon-carbon bond between the alpha- and beta-carbon
CC       of the two PPA units (PubMed:22627757). Sulfur-assisted furan ring
CC       formation, TE domain mediated hydrolysis, decarboxylation, and keto-
CC       enol tautomerization would generate microperfuranone attached to the T
CC       domain (PubMed:22627757). Finally, microperfuranone is released by the
CC       TE domain (PubMed:22627757). {ECO:0000269|PubMed:22627757}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:22627757}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; BN001306; CBF82791.1; -; Genomic_DNA.
DR   EMBL; AACD01000055; EAA63364.1; -; Genomic_DNA.
DR   RefSeq; XP_661000.1; XM_655908.1.
DR   AlphaFoldDB; Q5B7T4; -.
DR   SMR; Q5B7T4; -.
DR   STRING; 162425.CADANIAP00009643; -.
DR   ESTHER; emeni-q5b7t4; Thioesterase.
DR   EnsemblFungi; CBF82791; CBF82791; ANIA_03396.
DR   EnsemblFungi; EAA63364; EAA63364; AN3396.2.
DR   GeneID; 2874457; -.
DR   KEGG; ani:AN3396.2; -.
DR   VEuPathDB; FungiDB:AN3396; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_23_6_1; -.
DR   InParanoid; Q5B7T4; -.
DR   OMA; LWPAFGM; -.
DR   OrthoDB; 127131at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901512; P:(-)-microperfuranone biosynthetic process; IMP:AspGD.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..938
FT                   /note="Microperfuranone synthase"
FT                   /id="PRO_0000437582"
FT   DOMAIN          579..655
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          44..445
FT                   /note="Adenylation (A) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          581..652
FT                   /note="Thiolation and peptide carrier (T) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          676..923
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        746
FT                   /evidence="ECO:0000250|UniProtKB:A7XRY0"
FT   MOD_RES         613
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   938 AA;  103240 MW;  537E9EEE21712103 CRC64;
     MVGSVVEAHR QSVGCLRNLS QLLAWASNTS GGLIFYSRED DVLTSTRISY AELLADAGEK
     ARLIGQITGL SSESIILLHF DTQREVIEWF WAATLAGYLP AISTPFVDDT ARRKAHLLHL
     HAQLNQPVVL TSKRLVPEFL GLEELRLHDV ESLLSSAAKD GLIQYLGVQK LAEDVAVLML
     TSGSTGSAKA VPLRHGQLLT AIQGKSTHHG TLPGDVFYNW VGLDHVASLT EIHLHALILG
     SDQVHTAASE LLRNSLQFVR LLDTHKVAYT FAPNFFLTKV LDSLRENPTF TADLSSLKAL
     ISGGESNVVV TCDKLTRELR RRGVQAEVIR PGFGMTETCA GSIYSRACPS YDIRQSLEFA
     SLGSCIPGMH MRIMSITEPG KLAAPGESGE LQVAGPVVFD HYYNDETATR NAFTPDGWFI
     TGDLGWIDDA GNLNLAGRTK DTIIVNGVKW SSTELEAAIE EEAVSGLVRS FTVVVPTRPP
     GSATEEIAVV YSPAYAPEDY HARYETAQVI SKTVSLLTGT KPARLIPLPQ SLLEKSSLGK
     ISHSKVRAAL ESGEYASIER ADQLILAQYR QFKWRPAKSD SERAVQKALV EFLQVPAEGI
     NMDDSIYDLG VSSLNLILLR STLQRMLDPK IDIPLSIILN NPTPGAIARS IDSSRSSLAG
     YNAIVPLQQH RHGGTPLFCI HPGSGEVLVF VALAAHFPTR PVYALRTRGY GSNEQLFGSI
     EETVETYATQ IRQVQPHGPY AIAGYSLGST LAFEVAKVLE AQGEEVKFLA SIDYPPHIAH
     YVRDLNWTDV LLHIAFFLEL IDEKTMVEVT PYLHTLDRQT ALTHILNIGD AERARALAID
     TKHLGLISDI AENFRVNVKT YKPQGKVQHL DVFVADPPTY AARDRKDWRE NKLGRWVDFC
     ETKVEFHDCP GIHAKMLNRE HIAGFAKVFK AAMRRRGV