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Atrochrysone carboxyl ACP thioesterase (ACTE) (EC 3.1.-.-) (Endocrocin synthesis protein B)

 ENCB_ASPFU              Reviewed;         315 AA.
Q4W945;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
25-APR-2018, entry version 62.
RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000250|UniProtKB:Q0CCY4};
Short=ACTE {ECO:0000250|UniProtKB:Q0CCY4};
EC=3.1.-.- {ECO:0000250|UniProtKB:Q0CCY4};
AltName: Full=Endocrocin synthesis protein B {ECO:0000303|PubMed:22492455};
Name=encB {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00220;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
[2]
BIOTECHNOLOGY.
PubMed=20379952; DOI=10.1055/s-0030-1249779;
Gautam R., Karkhile K.V., Bhutani K.K., Jachak S.M.;
"Anti-inflammatory, cyclooxygenase (COX)-2, COX-1 inhibitory, and free
radical scavenging effects of Rumex nepalensis.";
Planta Med. 76:1564-1569(2010).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22492455; DOI=10.1128/AEM.07710-11;
Lim F.Y., Hou Y., Chen Y., Oh J.H., Lee I., Bugni T.S., Keller N.P.;
"Genome-based cluster deletion reveals an endocrocin biosynthetic
pathway in Aspergillus fumigatus.";
Appl. Environ. Microbiol. 78:4117-4125(2012).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23592999; DOI=10.1371/journal.ppat.1003289;
Berthier E., Lim F.Y., Deng Q., Guo C.J., Kontoyiannis D.P.,
Wang C.C., Rindy J., Beebe D.J., Huttenlocher A., Keller N.P.;
"Low-volume toolbox for the discovery of immunosuppressive fungal
secondary metabolites.";
PLoS Pathog. 9:E1003289-E1003289(2013).
[5]
INDUCTION.
PubMed=26242966; DOI=10.1111/1462-2920.13007;
Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
"Redundant synthesis of a conidial polyketide by two distinct
secondary metabolite clusters in Aspergillus fumigatus.";
Environ. Microbiol. 18:246-259(2016).
-!- FUNCTION: Atrochrysone carboxyl ACP thioesterase; part of the gene
cluster that mediates the biosynthesis of endocrocin, a simple
anthraquinone interesting for many biotechnological applications
(PubMed:22492455, PubMed:23592999). The pathway begins with the
synthesis of atrochrysone thioester by the polyketide synthase
(PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP
thioesterase encB then breaks the thioester bond and releases the
atrochrysone carboxylic acid from encA (PubMed:22492455). The
atrochrysone carboxylic acid is then converted to endocrocin
anthrone which is further oxidized into endocrocin by the anthrone
oxygenase encC (PubMed:22492455). The exact function of encD has
not been identified yet, but it negatively regulates endocrocin
production, likely through the modification of endocrocin itself
(PubMed:22492455). {ECO:0000269|PubMed:22492455,
ECO:0000269|PubMed:23592999}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q988B9};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q988B9};
-!- TISSUE SPECIFICITY: Endocrocin is specifically produced in
conidia. {ECO:0000305|PubMed:23592999}.
-!- INDUCTION: Expression is positively regulated by the transcription
factors brlA and laeA (PubMed:26242966).
{ECO:0000269|PubMed:26242966}.
-!- DISRUPTION PHENOTYPE: Abolishes the production of endocrocin
(PubMed:22492455). {ECO:0000269|PubMed:22492455}.
-!- BIOTECHNOLOGY: Endocrocin and related anthraquinones compounds
have interesting activities for medicinal uses, including anti-
inflammatory activity (PubMed:20379952).
{ECO:0000269|PubMed:20379952}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AAHF01000017; EAL84396.1; -; Genomic_DNA.
RefSeq; XP_746434.1; XM_741341.1.
ProteinModelPortal; Q4W945; -.
SMR; Q4W945; -.
STRING; 5085.CADAFUBP00009781; -.
EnsemblFungi; CADAFUAT00002486; CADAFUAP00002486; CADAFUAG00002486.
GeneID; 3503738; -.
KEGG; afm:AFUA_4G00220; -.
EuPathDB; FungiDB:Afu4g00220; -.
HOGENOM; HOG000246879; -.
InParanoid; Q4W945; -.
OMA; CAVGYPG; -.
OrthoDB; EOG092C4LEI; -.
Proteomes; UP000002530; Chromosome 4.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc.
CHAIN 1 315 Atrochrysone carboxyl ACP thioesterase.
/FTId=PRO_0000437053.
ACT_SITE 99 99 Proton donor/acceptor. {ECO:0000255}.
METAL 95 95 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 97 97 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 99 99 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 100 100 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
SEQUENCE 315 AA; 35346 MW; 73235EAF8EB23588 CRC64;
MDQYSNLFAF EDYLGAQARS IPDLPEVDVL SPRVVRVLGG NPGQMQLQGT NTYILGTGAE
RLLIDSGQGR ARWEQLMASL AAEHKFRIST VLLTHWHLDH TGGVPHLFRI FPELRGANAI
YKYHPDPSQQ AIVDGQVFSV EGATVRAVFT PGHSTDHMCF LLQEEEAIFT GDTVLGHGTT
GVEDLEEYMQ SLRKIQSLGC RIGYPGHGAV IENMQQKVQQ EIDRKQRRER QVLLALQNIQ
REKRTVGDAN GAATQAELIE AIFGRLPADV ADRFFAPYMK DILMKMARDK QVGFRFKGGQ
KHWFANVSQE NPVCR


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