PGDA_ARTBC
ID PGDA_ARTBC Reviewed; 437 AA.
AC D4B5F9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 {ECO:0000305};
DE Short=Peptidoglycan GlcNAc deacetylase {ECO:0000250|UniProtKB:Q8DP63};
DE EC=3.5.1.104 {ECO:0000250|UniProtKB:Q8DP63};
DE AltName: Full=Peptidoglycan N-deacetylase {ECO:0000250|UniProtKB:Q8DP63};
DE Short=PG N-deacetylase {ECO:0000250|UniProtKB:Q8DP63};
DE Flags: Precursor;
GN ORFNames=ARB_03699;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc)
CC residues in peptidoglycan. {ECO:0000250|UniProtKB:Q8DP63}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC glucosamine + acetate.; EC=3.5.1.104;
CC Evidence={ECO:0000250|UniProtKB:Q8DP63};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8DP63};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q8DP63};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE29445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000040; EFE29445.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003010085.1; XM_003010039.1.
DR AlphaFoldDB; D4B5F9; -.
DR SMR; D4B5F9; -.
DR STRING; 663331.D4B5F9; -.
DR EnsemblFungi; EFE29445; EFE29445; ARB_03699.
DR GeneID; 9525681; -.
DR KEGG; abe:ARB_03699; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_050708_0_0_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cobalt; Glycoprotein; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..437
FT /note="Probable peptidoglycan-N-acetylglucosamine
FT deacetylase ARB_03699"
FT /id="PRO_5003054702"
FT DOMAIN 149..334
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT DOMAIN 389..435
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 47..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT ACT_SITE 308
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT SITE 278
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000250|UniProtKB:Q8DP63"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 437 AA; 45972 MW; 3C3118F6722B3EC9 CRC64;
MLMRLYTFFA AALLACCAAA GPLHPELPQL VGKSWIPDWW FPFPRPSTRA ATTTTTPATS
TTGLATTTTK PTTTSSKPVT PTPQPATSTA QPAISSTANA TATATASSAS TSTTSSSTSA
STSTSAAAPS TPTTVVPFGQ VIRSCTVKGT VAITFDDGPY DYTNKLLDIF DANGAKATLF
VNAQNFGSIT DYSSVMLRAF NTGHQIASHT YDHADLSTLN GAGIISEMTK LDDVLATITN
GYRPTYMRVP YFAYSPLVLQ TMADLKYHVI EADIDTKDYE HDTPDGVSVS VGFFRDGLNA
GGSIALAHDV HQTTVDLLIQ QLLDEVKRRG LKAVTVGECL GDPRANWYRT TPVQVPTGTS
TTSPTATPTS PGTPPPAPTQ PGVASNCQKW HTVVSGDTCY DIAAANGISL DNLYKWNPAV
GTSCASLWLG YAVCVGV
