YANB_ASPNA
ID YANB_ASPNA Reviewed; 368 AA.
AC G3Y417;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Decarboxylase yanB {ECO:0000303|PubMed:24684908};
DE EC=4.1.1.52 {ECO:0000305|PubMed:24684908};
DE AltName: Full=Yanuthone D biosynthesis cluster protein B {ECO:0000303|PubMed:24684908};
GN Name=yanB {ECO:0000303|PubMed:24684908}; ORFNames=ASPNIDRAFT_44963;
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC 328 / USDA 3528.7;
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=11031048; DOI=10.1021/jo0006831;
RA Bugni T.S., Abbanat D., Bernan V.S., Maiese W.M., Greenstein M.,
RA Van Wagoner R.M., Ireland C.M.;
RT "Yanuthones: novel metabolites from a marine isolate of Aspergillus
RT niger.";
RL J. Org. Chem. 65:7195-7200(2000).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24684908; DOI=10.1016/j.chembiol.2014.01.013;
RA Holm D.K., Petersen L.M., Klitgaard A., Knudsen P.B., Jarczynska Z.D.,
RA Nielsen K.F., Gotfredsen C.H., Larsen T.O., Mortensen U.H.;
RT "Molecular and chemical characterization of the biosynthesis of the 6-MSA-
RT derived meroterpenoid yanuthone D in Aspergillus niger.";
RL Chem. Biol. 21:519-529(2014).
CC -!- FUNCTION: Decarboxylase; part of the gene cluster that mediates the
CC biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone
CC that acts as an antibiotic against fungi and bacteria
CC (PubMed:24684908). The first step of the pathway is the synthesis of 6-
CC methylsalicylic acid (6-MSA) by the polyketide synthase yanA
CC (PubMed:24684908). 6-MSA is then converted to m-cresol by the
CC decarboxylase yanB (PubMed:24684908). The cytochrome P450 monooxygenase
CC yanC then catalyzes the oxidation of m-cresol to toluquinol
CC (PubMed:24684908). Epoxidation of toluquinol is then performed by the
CC short chain dehydrogenase yanD, with the help of yanE, and a further
CC prenylation by yanG leads to 7-deacetoxyyanuthone A (PubMed:24684908).
CC The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by
CC the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A
CC (PubMed:24684908). O-Mevalon transferase yanI then attaches mevalon to
CC the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E
CC (PubMed:24684908). Finally, the FAD-dependent monooxygenase yanF
CC oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D
CC (PubMed:24684908). Furthermore, several branching points in the pathway
CC lead to the production of yanuthones F and G from 7-deacetoxyyanuthone
CC A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from
CC yanuthone E (PubMed:24684908). {ECO:0000269|PubMed:24684908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2;
CC Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52;
CC Evidence={ECO:0000305|PubMed:24684908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113;
CC Evidence={ECO:0000305|PubMed:24684908};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:24684908}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Loses the ability to produce yanuthone D
CC (PubMed:24684908). {ECO:0000269|PubMed:24684908}.
CC -!- BIOTECHNOLOGY: Yanuthone D is an antibiotic against C.albicans,
CC methicillin-resistant S.aureus (MRSA), and vancomycin-resistant
CC Enterococcus (PubMed:11031048). {ECO:0000269|PubMed:11031048}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; ACJE01000012; EHA22194.1; -; Genomic_DNA.
DR AlphaFoldDB; G3Y417; -.
DR SMR; G3Y417; -.
DR EnsemblFungi; EHA22194; EHA22194; ASPNIDRAFT_44963.
DR HOGENOM; CLU_039329_2_1_1; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047596; F:6-methylsalicylate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Glycoprotein; Lyase; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..368
FT /note="Decarboxylase yanB"
FT /id="PRO_0000436761"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 368 AA; 40345 MW; A2CA040D5D6F02A7 CRC64;
MDRIDVHHHF IPPAYVEAFK TTGGDPSGWH LPQWTPESSL SLMDSHNTRT AILSLTAPGT
SILAHSPGAS ATLAREINLY AAKLHNENPT RFGFFASLPH LTPDTIPAAI EEAIYALETL
HADGITLYTR YTGTGYLGHD AFAPLWEELN RRKAVVFIHP TNTAADARNR SILVNPALPQ
PIIDYPHETC RTAVDLITSG TISRNPDVKI ILSHGGGTLP ILATRAAHLL YDAKLTSISP
EDFLEQARSF YFDLALSGND ENMQLLVGRN GFAKGGHVFY GSDFPYAPVS TINKYVRMME
GFSVQGEEVE KAIARDSAVK LFPRFQMPAD LRVGKTNNWG AFSACLLLPV GLSALYSVLQ
SRVHTYST
