NSCB_ARTGP
ID NSCB_ARTGP Reviewed; 313 AA.
AC E4V2N5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=MGYG_06591;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
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).
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 The non-reducing polyketide synthase nscA probably synthesizes and
CC cyclizes the decaketide backbone (By similarity). The hydrolase nscB
CC then mediates the product release through hydrolysis followed by
CC spontaneous decarboxylation (By similarity). The prenyltransferase nscD
CC catalyzes the addition of the dimethylallyl group to the aromatic C5
CC (By similarity). The FAD-dependent monooxygenase nscC is then
CC responsible for the stereospecific hydroxylation at C2 (By similarity).
CC Neosartoricin B can be converted into two additional compounds
CC neosartoricins C and D (By similarity). Neosartoricin C is a
CC spirocyclic compound that is cyclized through the attack of C3 hydroxyl
CC on C14, followed by dehydration (By similarity). On the other hand,
CC neosartoricin D is a further cyclized compound in which attack of C2 on
CC C14 in neosartoricin C results in the formation of the acetal-
CC containing dioxabicyclo-octanone ring (By similarity). Both of these
CC compounds are novel and possibly represent related metabolites of the
CC gene cluster (By similarity). {ECO:0000250|UniProtKB:A1D8I9,
CC ECO:0000250|UniProtKB:F2S702, 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; DS989827; EFR03597.1; -; Genomic_DNA.
DR RefSeq; XP_003170605.1; XM_003170557.1.
DR AlphaFoldDB; E4V2N5; -.
DR SMR; E4V2N5; -.
DR STRING; 63402.XP_003170605.1; -.
DR EnsemblFungi; EFR03597; EFR03597; MGYG_06591.
DR GeneID; 10025844; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; E4V2N5; -.
DR OMA; VDHMCFV; -.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000002669; 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..313
FT /note="Lactamase-like protein nscB"
FT /id="PRO_0000437903"
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 313 AA; 34660 MW; D285FD67266F6907 CRC64;
MGGRLPFNQS FWEEFLMGRE GSLPNLPEIS HVSKRVVRIL GGNPGSMHLQ GTNTYLVGTG
RSRILIDTAQ GLPAWIHRIS SFLFTHNIEL SYVLLTHWHG DHTGGVPDLI AHNPLLTNKI
YKNNPDAGQN TITDGQIFSV NGATVRAVFT PGHSVDHMCF VLEEENALFT GDNVLGHGFS
VAQDLGCYMD SLRNMSALAC GLGYPAHGAI IENLPGKLDE YIQHREGRER MMLSTLTKEL
VQGQERRGEG TKGGLTLNEI VISIYGRLPQ EVIEKALAPS LLQVLWKLTE DRRVGFKPGD
PLKRQWFALI SVE
