NSCB_TRIEC
ID NSCB_TRIEC Reviewed; 331 AA.
AC F2PWS8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
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=TEQG_05349;
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97;
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; DS995747; EGE06346.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PWS8; -.
DR SMR; F2PWS8; -.
DR STRING; 63418.F2PWS8; -.
DR EnsemblFungi; EGE06346; EGE06346; TEQG_05349.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR Proteomes; UP000009169; 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_0000437900"
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
