ID   HEX1_COCPS              Reviewed;         595 AA.
AC   E9DFH0; Q309C3;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Beta-hexosaminidase 1;
DE            EC=3.2.1.52 {ECO:0000269|PubMed:20109094};
DE   AltName: Full=Beta-GlcNAcase 1 {ECO:0000305};
DE   AltName: Full=Beta-N-acetylhexosaminidase 1 {ECO:0000303|PubMed:20109094};
DE   AltName: Full=N-acetyl-beta-glucosaminidase 1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=HEX1 {ECO:0000303|PubMed:20109094}; ORFNames=CPSG_08485;
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=443226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=RMSCC 757 / Silveira;
RX   PubMed=20109094; DOI=10.3109/13693780903496609;
RA   Lunetta J.M., Johnson S.M., Pappagianis D.;
RT   "Molecular cloning, characterization and expression analysis of two beta-N-
RT   acetylhexosaminidase homologs of Coccidioides posadasii.";
RL   Med. Mycol. 48:744-756(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA   Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA   Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-hexosaminidase that shows a broad substrate specificity.
CC       {ECO:0000269|PubMed:20109094}.
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:0000269|PubMed:20109094};
CC   -!- INDUCTION: Expression is induced by N-acetylglucosamine.
CC       {ECO:0000269|PubMed:20109094}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; DQ232847; ABB18373.1; -; mRNA.
DR   EMBL; GL636503; EFW14827.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9DFH0; -.
DR   SMR; E9DFH0; -.
DR   STRING; 443226.E9DFH0; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   CLAE; HEX20A_COCPO; -.
DR   PRIDE; E9DFH0; -.
DR   EnsemblFungi; EFW14827; EFW14827; CPSG_08485.
DR   VEuPathDB; FungiDB:CPSG_08485; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   BRENDA; 3.2.1.52; 9184.
DR   Proteomes; UP000002497; Unassembled WGS sequence.
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; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..595
FT                   /note="Beta-hexosaminidase 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432745"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   595 AA;  68098 MW;  50132690A50F25E7 CRC64;
     MRFAYLATLA GSLLAGLAQA VKVNPLPAPQ HIKWGESGPQ YLDWNVKYSG PRDRTIIAAW
     RRTWGSIVQL RWTPAALEAP IPTFAPFIVG NGKRDAHSNR RILRVSVKVE NTNVDLQHGV
     DESYTLQIRD KSDSIRITAK TTWGVLRAFT TLQQIVIFKR GRFLVEQPVD IKDYPLYPVR
     GIMIDTARNF ISVKKIFEQL DGMALSKLNV LHWHITDTQS WPVEVRSYPQ MTEDAYSRRE
     TYGPSDIRKV IEYARARGIR VVPEIDMPGH SASGWRKIDP DIVACADSWW SNDDWEKHTA
     VQPNPGQLDI ANNKTYKVVE KVYNDISRIF TDDWFHVGGD ELQPNCFLTS KIVRDWLKQG
     SRTFNDLLQH WVDKTVPMMK KVKKNRRLLM WEDVLLSGNM HAHRVPRDII MQSWNGGLAN
     IKKLTARGYE VIVSSADFLY LDCGYGGWVG NDPRYNVMEN PDPETPNFNY GGNGGSWCGP
     YKTWQRIYNY DFTDGLNYAE KKRVIGAIAP LWSEQADDVV ISNKMWPRAA ALAELVWSGN
     VGKDGKKRTT LMTQRILNFR EYLVANGIMA APLQPKYCLK HPHSCDLYYD QTVIM