PKGB_EMENI
ID PKGB_EMENI Reviewed; 340 AA.
AC Q5AXB0; C8VB31;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Thioesterase pkgB {ECO:0000303|PubMed:22510154};
DE EC=3.1.2.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Pkg biosynthesis cluster protein B {ECO:0000303|PubMed:22510154};
GN Name=pkgB {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_07070;
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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
CC -!- FUNCTION: Thioesterase; part of the pkg gene cluster that mediates the
CC biosynthesis of dihydrocitreoisocoumarin and 6,8-dihydroxy-3-(2-
CC oxopropyl)-isocoumarin (PubMed:22510154). The non-reducing polyketide
CC synthase pkgA performs the condensation of one acetyl-CoA starter unit
CC with 6 and 5 malonyl-CoA units, respectively (PubMed:22510154). As pkgA
CC lacks a releasing domain, the thioesterase pkgB is necessary to break
CC the thioester bond and release dihydrocitreoisocoumarin and 6,8-
CC dihydroxy-3-(2-oxopropyl)-isocoumarin from pkgA (PubMed:22510154).
CC {ECO:0000269|PubMed:22510154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5,7,9,11,13-hexaoxotetradecanoyl-[ACP] =
CC dehydrocitreoisocoumarin + H2O + holo-[ACP]; Xref=Rhea:RHEA:64492,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:15846, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:142800, ChEBI:CHEBI:155857;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64493;
CC Evidence={ECO:0000269|PubMed:22510154};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,5,7,9,11-pentaoxododecanoyl-[ACP] = 6,8-dihydroxy-3-(2-
CC oxopropyl)-isocoumarin + H2O + holo-[ACP]; Xref=Rhea:RHEA:64496,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16607, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:155858, ChEBI:CHEBI:155859;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64497;
CC Evidence={ECO:0000269|PubMed:22510154};
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 -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; BN001304; CBF79145.1; -; Genomic_DNA.
DR RefSeq; XP_664674.1; XM_659582.1.
DR AlphaFoldDB; Q5AXB0; -.
DR SMR; Q5AXB0; -.
DR STRING; 162425.CADANIAP00000399; -.
DR EnsemblFungi; CBF79145; CBF79145; ANIA_07070.
DR EnsemblFungi; EAA61199; EAA61199; AN7070.2.
DR GeneID; 2869946; -.
DR KEGG; ani:AN7070.2; -.
DR VEuPathDB; FungiDB:AN7070; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; Q5AXB0; -.
DR OMA; VDHMCFV; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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..340
FT /note="Thioesterase pkgB"
FT /id="PRO_0000450872"
FT REGION 242..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
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="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 101
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 102
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 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 340 AA; 36629 MW; 46E107E49DC1A50F CRC64;
MSGGFYSSPF WAGYLETQRS RLPVLPEIDD GLSHCVVRFL GYNPGSMQLQ GTNTYLVGTG
STRILIDTGE GAPQWAVSVT RYLEDHDISI SHVLLTHWHK DHTGGVADLL AHDPSIIVYK
HAPDPGQQAI ANGQTFKTQG ATLRAVLTPG HAVDHMCFLL EEENALFTGD NVLGHGYSVA
EDLETYTASL RLMAGLKCSV GYPGHGDAIL NLPQTIARYI SQRVAREKKI YAILALHACS
CSSRNGGSTS SIGSVSESGD SDEEDNNMKT SRPAMQGLST AEIGGLVYGE SVKNSPTFDS
AVGPLLNQVL YMLLEQGKCC DHVSILVIFQ KPGFFSIPVI
