NSCB_TRIRC
ID NSCB_TRIRC Reviewed; 322 AA.
AC F2T0M3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
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=TERG_08360;
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892;
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: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}.
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DR EMBL; GG700661; EGD92145.1; -; Genomic_DNA.
DR RefSeq; XP_003231062.1; XM_003231014.1.
DR AlphaFoldDB; F2T0M3; -.
DR SMR; F2T0M3; -.
DR STRING; 559305.F2T0M3; -.
DR EnsemblFungi; EGD92145; EGD92145; TERG_08360.
DR GeneID; 10377338; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR InParanoid; F2T0M3; -.
DR Proteomes; UP000008864; 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; Reference proteome; Zinc.
FT CHAIN 1..322
FT /note="Lactamase-like protein nscB"
FT /id="PRO_0000437904"
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 322 AA; 35972 MW; 1E35F9FA3DBF8946 CRC64;
MSGRLPFSQS FWEEFLMGRE GHLPVLPELS HVSKGVIRIL GGNPGSMHLQ GTNTYLVGTG
RSRILIDTAQ GLPAWINRIS SFLSTQKIEL SYVLLTHWHG DHTGGVPDLI ARNSSLANKI
YKNQPDSGQS PITHGQIFSV DGATVRAILT PGHSVDHMCF LLEEENALFT GDNVLGHGFS
VAQDLGRYMD SLRDMASLGC RIGYPAHGAM IENLPGKLEE YIQHREGRER MMLSALTRHR
VRGEGTRDER VKYGLTLNEI VLAVYGRLPQ EVIEKALAPS LLQVLWKLTE DRMVGFKPGD
PLKRQWFALE QRQRNKVRGC RG
