ENCB_ASPFU
ID ENCB_ASPFU Reviewed; 315 AA.
AC Q4W945;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000250|UniProtKB:Q0CCY4};
DE Short=ACTE {ECO:0000250|UniProtKB:Q0CCY4};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:Q0CCY4};
DE AltName: Full=Endocrocin synthesis protein B {ECO:0000303|PubMed:22492455};
GN Name=encB {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00220;
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 BIOTECHNOLOGY.
RX PubMed=20379952; DOI=10.1055/s-0030-1249779;
RA Gautam R., Karkhile K.V., Bhutani K.K., Jachak S.M.;
RT "Anti-inflammatory, cyclooxygenase (COX)-2, COX-1 inhibitory, and free
RT radical scavenging effects of Rumex nepalensis.";
RL Planta Med. 76:1564-1569(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22492455; DOI=10.1128/aem.07710-11;
RA Lim F.Y., Hou Y., Chen Y., Oh J.H., Lee I., Bugni T.S., Keller N.P.;
RT "Genome-based cluster deletion reveals an endocrocin biosynthetic pathway
RT in Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 78:4117-4125(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23592999; DOI=10.1371/journal.ppat.1003289;
RA Berthier E., Lim F.Y., Deng Q., Guo C.J., Kontoyiannis D.P., Wang C.C.,
RA Rindy J., Beebe D.J., Huttenlocher A., Keller N.P.;
RT "Low-volume toolbox for the discovery of immunosuppressive fungal secondary
RT metabolites.";
RL PLoS Pathog. 9:E1003289-E1003289(2013).
RN [5]
RP INDUCTION.
RX PubMed=26242966; DOI=10.1111/1462-2920.13007;
RA Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
RT "Redundant synthesis of a conidial polyketide by two distinct secondary
RT metabolite clusters in Aspergillus fumigatus.";
RL Environ. Microbiol. 18:246-259(2016).
CC -!- FUNCTION: Atrochrysone carboxyl ACP thioesterase; part of the gene
CC cluster that mediates the biosynthesis of endocrocin, a simple
CC anthraquinone interesting for many biotechnological applications
CC (PubMed:22492455, PubMed:23592999). The pathway begins with the
CC synthesis of atrochrysone thioester by the polyketide synthase (PKS)
CC encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB
CC then breaks the thioester bond and releases the atrochrysone carboxylic
CC acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is
CC then converted to endocrocin anthrone which is further oxidized into
CC endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact
CC function of encD has not been identified yet, but it negatively
CC regulates endocrocin production, likely through the modification of
CC endocrocin itself (PubMed:22492455). {ECO:0000269|PubMed:22492455,
CC ECO:0000269|PubMed:23592999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64236, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149712, ChEBI:CHEBI:149713;
CC Evidence={ECO:0000250|UniProtKB:Q0CCY4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000250|UniProtKB:Q0CCY4};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
CC -!- TISSUE SPECIFICITY: Endocrocin is specifically produced in conidia.
CC {ECO:0000305|PubMed:23592999}.
CC -!- INDUCTION: Expression is positively regulated by the transcription
CC factors brlA and laeA (PubMed:26242966). {ECO:0000269|PubMed:26242966}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of endocrocin
CC (PubMed:22492455). {ECO:0000269|PubMed:22492455}.
CC -!- BIOTECHNOLOGY: Endocrocin and related anthraquinones compounds have
CC interesting activities for medicinal uses, including anti-inflammatory
CC activity (PubMed:20379952). {ECO:0000269|PubMed:20379952}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AAHF01000017; EAL84396.1; -; Genomic_DNA.
DR RefSeq; XP_746434.1; XM_741341.1.
DR AlphaFoldDB; Q4W945; -.
DR SMR; Q4W945; -.
DR STRING; 746128.CADAFUBP00009781; -.
DR EnsemblFungi; EAL84396; EAL84396; AFUA_4G00220.
DR GeneID; 3503738; -.
DR KEGG; afm:AFUA_4G00220; -.
DR VEuPathDB; FungiDB:Afu4g00220; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; Q4W945; -.
DR OMA; VDHMCFV; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..315
FT /note="Atrochrysone carboxyl ACP thioesterase"
FT /id="PRO_0000437053"
FT ACT_SITE 99
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ 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
