ID   HEX1_ARTBC              Reviewed;         605 AA.
AC   D4AUH6;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Beta-hexosaminidase ARB_07893 {ECO:0000305};
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-GlcNAcase ARB_07893 {ECO:0000305};
DE   AltName: Full=Beta-N-acetylhexosaminidase ARB_07893 {ECO:0000305};
DE   AltName: Full=N-acetyl-beta-glucosaminidase ARB_07893 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_07893;
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: Beta-hexosaminidase that shows a broad substrate specificity
CC       (By similarity). {ECO:0000250|UniProtKB:E9DFH0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000250|UniProtKB:E9DFH0};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; ABSU01000011; EFE33141.1; -; Genomic_DNA.
DR   RefSeq; XP_003013781.1; XM_003013735.1.
DR   AlphaFoldDB; D4AUH6; -.
DR   SMR; D4AUH6; -.
DR   STRING; 663331.D4AUH6; -.
DR   EnsemblFungi; EFE33141; EFE33141; ARB_07893.
DR   GeneID; 9526972; -.
DR   KEGG; abe:ARB_07893; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   OMA; GHDVVMC; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.379.10; -; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR029019; HEX_eukaryotic_N.
DR   PANTHER; PTHR22600; PTHR22600; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF14845; Glycohydro_20b2; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..605
FT                   /note="Beta-hexosaminidase ARB_07893"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434663"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   ACT_SITE        374
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR001093-1"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   605 AA;  68518 MW;  7EED327E46952C2F CRC64;
     MLWIWVPGIL GLFGRVEALW PQPSEYSHGN KTLWLSPSVR FTYTNNQRSF IYTRPSYAGI
     NWIPGGWLNL LQNPWGSAEQ TVAEPLPNVE QFVEDAIKRT KHAIINSKFV PWKFHPRHQK
     FEPLVDGQHP TIEEVIINEA SKTSQEWSPR NYVNGDEKYE IRISEDGEVQ ISSRSPIGTI
     RALQTFQQLF YSHSHSKSYT PFAPISISDS PKWRHRGLNL DISRNVIRPE DVKRTIDAMA
     SVKLNRLHAH AADSQSWPLD IPSIPELAAK ASYHPSQVWS SSELEAVQLY GLERGVSVFL
     EIDLPGHTAA VGHAFPDLVA AYHMDQWEKY AAEPPSGQIK LNSSAVYQFL DLLMADLIPR
     VSPLTEYFHT GGDEFNLNTY LLEINLGSND RRVLTPFLDR MITHVHSSLR SSGVTPIVWE
     ELVLDWDLNL PSHKTAGETG GVIVQAWRNS SAVKHVLQKG YQTIFGTGDA WYLDCGVGTF
     LNPRPGSKAV QNPYLDWCAP TKNWKHMYVY NPLKDIPVEL QSLLVGGETH MWSELVDPVN
     MDQMIWPRAA AAAEVLWTGP RSPDNIQDAS YRLAKWRERV VNDAGIRAAM VQMTYCLMRE
     SGCEL