APTB_EMENI
ID APTB_EMENI Reviewed; 309 AA.
AC Q5B0C9; C8V345;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lactamase-like protein aptB {ECO:0000303|PubMed:18978088};
DE EC=3.1.-.- {ECO:0000269|PubMed:21866960, ECO:0000305|PubMed:18978088};
DE AltName: Full=Asperthecin synthesis protein B {ECO:0000303|PubMed:18978088};
GN Name=aptB {ECO:0000303|PubMed:18978088}; ORFNames=AN6001.2;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=18978088; DOI=10.1128/aem.01743-08;
RA Szewczyk E., Chiang Y.M., Oakley C.E., Davidson A.D., Wang C.C.,
RA Oakley B.R.;
RT "Identification and characterization of the asperthecin gene cluster of
RT Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 74:7607-7612(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21866960; DOI=10.1021/ja206906d;
RA Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT "Comparative characterization of fungal anthracenone and naphthacenedione
RT biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT cyclization catalyzed by a dimanganese thioesterase.";
RL J. Am. Chem. Soc. 133:15773-15785(2011).
RN [5]
RP INDUCTION.
RX PubMed=26773375; DOI=10.1016/j.fgb.2016.01.004;
RA Bayram O., Feussner K., Dumkow M., Herrfurth C., Feussner I., Braus G.H.;
RT "Changes of global gene expression and secondary metabolite accumulation
RT during light-dependent Aspergillus nidulans development.";
RL Fungal Genet. Biol. 87:30-53(2016).
CC -!- FUNCTION: Lactamase-like protein; part of the gene cluster that
CC mediates the biosynthesis of asperthecin, an anthraquinone pigment
CC (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA
CC catalyzes the formation of the aromatic polyketide from acetyl coenzyme
CC A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide
CC is subsequently hydrolyzed by the action of aptB into endocrocin-9-
CC anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into
CC endocrocin by aptC (PubMed:18978088). Endocrocin is likely to
CC decarboxylate spontaneously to form emodin which explains why there is
CC no decarboxylase in the asperthecin biosynthesis cluster
CC (PubMed:18978088). Finally, aptC or another endogenous oxygenase
CC catalyzes additional oxidation steps to form asperthecin.
CC {ECO:0000269|PubMed:18978088, ECO:0000269|PubMed:21866960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3,6,8,9-pentahydroxy-1-oxo-3-(2-oxopropyl)-1,2,3,4-
CC tetrahydroanthracene-2-carboxyl-[ACP] + H2O = 2,3,6,8,9-pentahydroxy-
CC 1-oxo-3-(2-oxopropyl)-1,2,3,4-tetrahydroanthracene-2-carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64080, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16517, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149683, ChEBI:CHEBI:149686;
CC Evidence={ECO:0000269|PubMed:21866960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64081;
CC Evidence={ECO:0000269|PubMed:21866960};
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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:18978088}.
CC -!- INDUCTION: Expression is induced during late sexual development in the
CC dark (PubMed:26773375). {ECO:0000269|PubMed:26773375}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce asperthecin (PubMed:18978088).
CC {ECO:0000269|PubMed:18978088}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; BN001301; CBF70385.1; -; Genomic_DNA.
DR EMBL; AACD01000102; EAA57750.1; -; Genomic_DNA.
DR RefSeq; XP_663605.1; XM_658513.1.
DR AlphaFoldDB; Q5B0C9; -.
DR SMR; Q5B0C9; -.
DR STRING; 162425.CADANIAP00007017; -.
DR EnsemblFungi; CBF70385; CBF70385; ANIA_06001.
DR EnsemblFungi; EAA57750; EAA57750; AN6001.2.
DR GeneID; 2871042; -.
DR KEGG; ani:AN6001.2; -.
DR VEuPathDB; FungiDB:AN6001; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; Q5B0C9; -.
DR OMA; PAKLIVW; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036184; P:asperthecin 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..309
FT /note="Lactamase-like protein aptB"
FT /id="PRO_0000436111"
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"
SQ SEQUENCE 309 AA; 34674 MW; A01B77F468024A4A CRC64;
MAFRIPFAQD FWNEYLSGRE NTIPTLPVVT DITERVIRVL GGNAGPMRLQ GTNTYLVGTG
RSRILVDTGQ GMPSWIRDIA KVLEERDIDI SYVLLTHWHG DHTGGVPDLI AYNPALSSRI
YKNRPDAGQK DILDGQVFRV EGATLRAVHT PGHAADHMCF LFEEENALFT GDNVLGHGYS
VVEDLGQYMN SMVQMANLNL PLGYPAHGAV IDDLPDKMRE YIKHREFRVQ QVYAILEESR
AAGQGRGRGG LTLHEIILAM YGEITDEVEK ALAPFLSQVL WKLAEDRKVG FEPGSAAKRR
WYVRSRRPN
