HEX1_CANAX
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 03-AUG-2022, entry version 92.
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 VEuPathDB; FungiDB:C5_03610W_A; -.
DR VEuPathDB; FungiDB:CAWG_04734; -.
DR PHI-base; PHI:4987; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 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