ID   E1Z7G7_CHLVA            Unreviewed;       550 AA.
AC   E1Z7G7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=CHLNCDRAFT_141982 {ECO:0000313|EMBL:EFN57917.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN57917.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN57917.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL433838; EFN57917.1; -; Genomic_DNA.
DR   RefSeq; XP_005850019.1; XM_005849957.1.
DR   AlphaFoldDB; E1Z7G7; -.
DR   STRING; 554065.E1Z7G7; -.
DR   GeneID; 17357595; -.
DR   KEGG; cvr:CHLNCDRAFT_141982; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   InParanoid; E1Z7G7; -.
DR   OMA; KMWPRAA; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000008141; 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; 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   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|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..550
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003156037"
FT   DOMAIN          96..145
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          167..506
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        328
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   550 AA;  59908 MW;  F24674103277F3DC CRC64;
     MLVAMLLHVL LLSGPQQARA DSEAPMVWPR PASLSHGACN GGSPLGLAGA QLQVRVLSGQ
     ADEATAYVEA ALQAALPEWG CGIEAGPAAT GPTISVVIAN ASCTQPSCYS HENDESYSLQ
     IDEAGAITIA AAEIFGANWA LSTLSSLANG TCGLTCLPIE VEDTPRFGHR GVLVDTARHW
     FSVEDLKRKI LDPMHATKMN VLHWHVYDSQ SQPLELRFDP RLWLPYSKEQ RFTQEDAREV
     VRYAFARGIR VLPEFDLPGH TAIFGKADPG LVDCLDYLPW DGTGVPNVMA NQPPAGQLKP
     DQAGLASQLL DEMMELFPNS IISSGADEVN FNCWNNATVV AQNASDYPQF QEKMVRKLAG
     FQEQVAATIN GAGRTMAVWD ESYGTWNFSG TPALPRGSVL LSWLDTNNTA AMTDAGYNVV
     WMPWRRLYLD CGLGTPTSPP NWCAPLNNWT TIYLANPLET FNATSGDPSR LLGAEVATWS
     EHIVPSILDY VVWPRAAALA ERLWSPEKDT QWCDTAPPQL NSEGVDYCAP AKTYKGVDLT
     FDNLVDPKEV
//