ID Q22C96_TETTS Unreviewed; 564 AA.
AC Q22C96;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=TTHERM_01068140 {ECO:0000313|EMBL:EAR82911.1};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR82911.1, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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:0000256|ARBA:ARBA00001231,
CC ECO:0000256|PIRNR:PIRNR001093};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR EMBL; GG662550; EAR82911.1; -; Genomic_DNA.
DR RefSeq; XP_001030574.1; XM_001030574.1.
DR AlphaFoldDB; Q22C96; -.
DR STRING; 312017.Q22C96; -.
DR EnsemblProtists; EAR82911; EAR82911; TTHERM_01068140.
DR GeneID; 7831150; -.
DR KEGG; tet:TTHERM_01068140; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_3_1; -.
DR InParanoid; Q22C96; -.
DR OMA; GHDVVMC; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000009168; 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 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 PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF00728; Glyco_hydro_20; 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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001093};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..564
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004200641"
FT DOMAIN 185..518
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 348
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 564 AA; 64426 MW; 862E1299006FBC3A CRC64;
MQKSIIIAAI LLVGLASALR IVPVPQNLQK GNFTFEVASI DSVEFQFKTS GRLNELSSVQ
QRILESQNEQ NLRKFKSIAH EKLDERLSKL KVAQAKNGLK GANLVVKVFL NNTDTQYTSY
DNFKIDEAYE ISINQNLTNI EFKCHGYVSF LRAIETFIQI LIQSHQKTHF AFDFLPLSIN
DAPAFGHRGV MIDTSRHFLS LEAIKQTIRG LSISKFNVLH LHLTDSESFP FELFSYPEIT
AFGAYSPEEI YTQEELRELD AYSQTYGVIL IPEIDSPAHT RSWSNPPNLQ DIDACRDYPK
EQWGLFCNEP PCGQLDVTLE KARTVAADIM VETARIFSSE FLHLGGDEPN KHCWETKASI
AEYMKANNIS NYNELQTFYR DFQKEVIEQN NLNKKRIFWL ASNNVDVQTD DQAIMQFWGD
LDEYSYMLKV NNPVILSTYT YLYLDCGLGN TFGDNSWCDP YKTWKRIYSF DVTAGNLISR
ERNLGSEAAI WTETSTTDDF VQKLFPRVIA LSLNLWNPEA KLADIELVKH LVAIKDSIRL
AGIPTGAVSS QYCELNVEHC FFEN
//
