NSCB_ARTBC
ID NSCB_ARTBC Reviewed; 439 AA.
AC D4AWH0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=ARB_00535;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:A1D8J2,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABSU01000014; EFE32710.1; -; Genomic_DNA.
DR RefSeq; XP_003013350.1; XM_003013304.1.
DR AlphaFoldDB; D4AWH0; -.
DR SMR; D4AWH0; -.
DR STRING; 663331.D4AWH0; -.
DR EnsemblFungi; EFE32710; EFE32710; ARB_00535.
DR GeneID; 9519385; -.
DR KEGG; abe:ARB_00535; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OMA; PAKLIVW; -.
DR Proteomes; UP000008866; 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..439
FT /note="Lactamase-like protein nscB"
FT /id="PRO_0000437901"
FT ACT_SITE 218
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 214
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 216
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 218
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 219
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 439 AA; 49014 MW; 28DBB3F35F17365B CRC64;
MKSRVYVRFD RGFHVICPYQ AKLAGSRKND GAGYISPLAL KSPIGLQHDL EDGCRIRSAF
GKCIVNSRFL ALIDVRKSGF KERGSKEPHG NSFVYWVTYS FLQFFETTMD ELPSGRGMGG
RLPFNQSFWE EFLSGREGQL PTLPDISHVS KSVIRILGGN PGSMHLQGTN TYLVGTGRSR
ILIDTAQGLP VWIDCISSFL HTQKIELSYV LLTHWHGDHT GGVPDLIAQN SSLADKIYKN
HPDSGQNPIT HGQIFSVDGA TVRAIFTPGH SVDHMCFLLE EENALFTGDN VLGHGFSVAQ
DLGRYMDSLR DMASLGCRIG YPAHGAVIEN LPGKLEEYIQ HREGRERMML SALTRQRVRG
EGLREEGVKC GLTLNEIVMA IYGKLPPEVI EKALAPSLLQ VLWKLTEDRM VGFKPGDPLK
RQWFALEQRK RNKARGYPS
