NSCB_TRIT1
ID NSCB_TRIT1 Reviewed; 331 AA.
AC F2S702;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Lactamase-like protein nscB {ECO:0000303|PubMed:23758576};
DE EC=3.1.-.- {ECO:0000305|PubMed:23758576};
DE AltName: Full=Neosartoricin B biosynthesis protein B {ECO:0000303|PubMed:23758576};
GN Name=nscB {ECO:0000303|PubMed:23758576}; ORFNames=TESG_06705;
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
RN [2]
RP FUNCTION.
RX PubMed=23758576; DOI=10.1021/sb400048b;
RA Yin W.B., Chooi Y.H., Smith A.R., Cacho R.A., Hu Y., White T.C., Tang Y.;
RT "Discovery of cryptic polyketide metabolites from dermatophytes using
RT heterologous expression in Aspergillus nidulans.";
RL ACS Synth. Biol. 2:629-634(2013).
RN [3]
RP FUNCTION.
RX PubMed=23368997; DOI=10.1021/ol303435y;
RA Chooi Y.H., Fang J., Liu H., Filler S.G., Wang P., Tang Y.;
RT "Genome mining of a prenylated and immunosuppressive polyketide from
RT pathogenic fungi.";
RL Org. Lett. 15:780-783(2013).
CC -!- FUNCTION: Lactamase-like protein; part of the gene cluster that
CC mediates the biosynthesis of neosartoricin B, a prenylated anthracenone
CC that probably exhibits T-cell antiproliferative activity, suggestive of
CC a physiological role as an immunosuppressive agent (PubMed:23758576,
CC PubMed:23368997). The non-reducing polyketide synthase nscA probably
CC synthesizes and cyclizes the decaketide backbone (By similarity). The
CC hydrolase nscB then mediates the product release through hydrolysis
CC followed by spontaneous decarboxylation (By similarity). The
CC prenyltransferase nscD catalyzes the addition of the dimethylallyl
CC group to the aromatic C5 (By similarity). The FAD-dependent
CC monooxygenase nscC is then responsible for the stereospecific
CC hydroxylation at C2 (By similarity). Neosartoricin B can be converted
CC into two additional compounds neosartoricins C and D (PubMed:23758576).
CC Neosartoricin C is a spirocyclic compound that is cyclized through the
CC attack of C3 hydroxyl on C14, followed by dehydration
CC (PubMed:23758576). On the other hand, neosartoricin D is a further
CC cyclized compound in which attack of C2 on C14 in neosartoricin C
CC results in the formation of the acetal-containing dioxabicyclo-octanone
CC ring (PubMed:23758576). Both of these compounds are novel and possibly
CC represent related metabolites of the gene cluster (PubMed:23758576).
CC {ECO:0000250|UniProtKB:A1D8J2, ECO:0000269|PubMed:23758576,
CC ECO:0000305|PubMed:23368997}.
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:23758576}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; GG698521; EGD99351.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S702; -.
DR SMR; F2S702; -.
DR EnsemblFungi; EGD99351; EGD99351; TESG_06705.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000009172; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001018; Beta-lactamase_class-B_CS.
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.
DR PROSITE; PS00743; BETA_LACTAMASE_B_1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..331
FT /note="Lactamase-like protein nscB"
FT /id="PRO_0000437899"
FT ACT_SITE 110
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 106
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 108
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 110
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 111
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 331 AA; 36643 MW; A926D9F9B6801430 CRC64;
MDQSSSGGSM GGRLPFNQSF WEEFLMGREG HLPALPEISH VSKSVVRILG GNPGSMHLQG
TNTYLVGTGR SRILIDTAQG LPVWISRISS FLYTQKIELS YVLLTHWHGD HTGGVPDLIS
QNSSLSNRIY KNRPDSGQNP ITHGQIFSVA GATVRAILTP GHSVDHMCFL LEEENALFTG
DNVLGHGFSV AQDLGRYMDS LRDMASLGCR IGYPAHGAVI EKLPGKLEEY IQHREGRERM
MLSALTRQRV QGEGVREGGV KCGLTLNEIV MVIYGRLPQE VIEKALAPSL LQVLWKLTED
RMVGFKPGDP LKRQWFALEQ KKRNKVRGCP S
