NSCB_ARTOC
ID NSCB_ARTOC Reviewed; 343 AA.
AC C5FM60;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=MCYG_03601;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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 (By similarity).
CC Neosartoricin C is a spirocyclic compound that is cyclized through the
CC attack of C3 hydroxyl on C14, followed by dehydration (By similarity).
CC On the other hand, neosartoricin D is a further cyclized compound in
CC which attack of C2 on C14 in neosartoricin C results in the formation
CC of the acetal-containing dioxabicyclo-octanone ring (By similarity).
CC Both of these compounds are novel and possibly represent related
CC metabolites of the gene cluster (By similarity).
CC {ECO:0000250|UniProtKB:A1D8J2, ECO:0000250|UniProtKB:F2S702,
CC ECO:0000305|PubMed:23368997, ECO:0000305|PubMed:23758576}.
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:0000305|PubMed:23758576}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; DS995703; EEQ30782.1; -; Genomic_DNA.
DR RefSeq; XP_002848095.1; XM_002848049.1.
DR AlphaFoldDB; C5FM60; -.
DR SMR; C5FM60; -.
DR STRING; 63405.XP_002848095.1; -.
DR EnsemblFungi; EEQ30782; EEQ30782; MCYG_03601.
DR GeneID; 9229417; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OMA; VDHMCFV; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000002035; 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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..343
FT /note="Lactamase-like protein nscB"
FT /id="PRO_0000437898"
FT ACT_SITE 122
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 118
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 120
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 122
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 123
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 343 AA; 38096 MW; 76AF53E9DC628705 CRC64;
MGGRMPFNQS FWEEFLMGRE GRLPTLPEIS HVSKRVVRIL GGNPGSMHLQ GTNTYLVGTG
RSRILIDTAQ VKQASFLRLQ RAPSQLIHSK KGLPVWISRI SSFLRTHNLE LSYVLLTHWH
GDHTGGVPDL LAHSPSLADK IYKNCPDAGQ NPITDGQIFS VNGATVRAVF TPGHSVDHMC
FQLEEENALF TGDNVLGHGF SVAQDLGRYM HSLGDMASLG CGIGYPAHGA VIGNLPEKLE
EYMKHREGRE RMMLSTLTRE QAQGEGGRVG ETKGGLTLNE IVIAMYGRVP QEVVEKALAP
SLLQVLWKLA EDRRVGFKPG DPLKRRWFAL DQRKRNRVRG YPS
