ID   HEX1_CANAX              Reviewed;         562 AA.
AC   P43077;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Beta-hexosaminidase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-GlcNAcase;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   Flags: Precursor;
GN   Name=HEX1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-42.
RC   STRAIN=A72;
RX   PubMed=8169213; DOI=10.1128/jb.176.9.2640-2647.1994;
RA   Cannon R.D., Niimi K., Jenkinson H.F., Shepherd M.G.;
RT   "Molecular cloning and expression of the Candida albicans beta-N-
RT   acetylglucosaminidase (HEX1) gene.";
RL   J. Bacteriol. 176:2640-2647(1994).
CC   -!- FUNCTION: Has a broad substrate specificity.
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   -!- INDUCTION: By growth on N-acetylglucosamine.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; L26488; AAA34346.2; -; Genomic_DNA.
DR   PIR; A55588; A55588.
DR   AlphaFoldDB; P43077; -.
DR   SMR; P43077; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   CLAE; HEX20A_CANAL; -.
DR   GlyCosmos; P43077; 7 sites, No reported glycans.
DR   VEuPathDB; FungiDB:C5_03610W_A; -.
DR   VEuPathDB; FungiDB:CAWG_04734; -.
DR   PHI-base; PHI:4987; -.
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   CDD; cd06562; GH20_HexA_HexB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8169213"
FT   CHAIN           23..562
FT                   /note="Beta-hexosaminidase"
FT                   /id="PRO_0000012014"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   562 AA;  63491 MW;  CC70FEA69FB3E836 CRC64;
     MVLDKMIIFH LLLWLCNVVV HAAKVEILPA PQSVTWENDT AIIINPRLLQ ANTSCPLLED
     AFVRTVSAIE KSKWHPFPID DFNTANGKNI KTSLVHIQVD DATVDLQLGV NESYTLKINT
     DGINIHAATT WGALHGLVSL QQLIIHTSED KYVVPSSVTI SDFPNFKHRG LMIDSGRNFL
     TVDSILEQID IMALSKMNSL HWHLADSQSW PVALESYPHM IKDAYSNDEV YSKNDLKYIV
     DYARARGVRV IPEIDMPGHA RAGWKQVDPT IVECADAFWT DAAVEPPPGQ LNIESEKTYE
     VISNVYNELS DIFIDDVFHV GNDELQEKCY SAQLSPNNTV TDLLKRYLKK ALPIFNKVNH
     RKLTMWDDVL LSDVSADKIP SNITLQVWHE ISGVKNLTSR GYDVVVSSSD FLYLDCGNAG
     WVTNDPRYVE TPENVDFNTG QGGSWCGPYK SYQRIYNFDF TANLTETEKN HVLGREAALW
     SEQVDSTVLT TKIWPRTAAL AELTWSGNKD SNGHHRGYEF TQRILNFREY LVKLGYGVSP
     LVPKYCLLNP HACDLYKNPP VY
//