ID   D2V634_NAEGR            Unreviewed;       634 AA.
AC   D2V634;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=NAEGRDRAFT_64295 {ECO:0000313|EMBL:EFC47760.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC47760.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC47760.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(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         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; GG738853; EFC47760.1; -; Genomic_DNA.
DR   RefSeq; XP_002680504.1; XM_002680458.1.
DR   AlphaFoldDB; D2V634; -.
DR   STRING; 5762.D2V634; -.
DR   EnsemblProtists; EFC47760; EFC47760; NAEGRDRAFT_64295.
DR   GeneID; 8861924; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_64295; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   InParanoid; D2V634; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000006671; 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   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:UP000006671};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..634
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003038472"
FT   DOMAIN          184..493
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          557..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        340
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   634 AA;  71111 MW;  919F4542A31E7AAD CRC64;
     MLKLLLSVIC FLCLTSGVLI TTSTAATTVT LDANNLSIWP QPQIIKNYEN KPSLEFTRIC
     FNVSSFISSD WNNLAECERN FLSNALNRLS TRYQFIGPSN SSSCVKFSLK KETSSCKISL
     LNSSEKYEMW LNGNYSTIKA ENVFGTLRAI QTLAQIIDQA YSIVKNAKSQ VIISSIYIQD
     YPFYNYRGLM LDTARHFIAV DSLKRHIDSM EEVKMNAFHL HITDDESFPI NMTKYSPSTY
     KFNGGPLTFE ILRDLNEYCA DRGIQFIPEI DTPSHSQSWS TYYPSIMYPS CTNHLDMGKQ
     ETYQVVANVY QFLFKLLGSW TQTIPRIKFT NQFLHAGFDE IDGNCYSNDA TLKKYQTFVL
     NNILQNGSLI ASGDSTDKIL PIVWADDLIT DYQLGNTSAL PRDTILQIWR NDATLTETLK
     YYYKTIVSIS EPWYIDAPCS RTFEKIYQYK PPAHPSVIGG STCMWTSSGD TDNDLEEYVW
     PRAAAVAERL WTNPCNPITF WNASFPYNTQ KLSRKTILTN RIVKTGTAAQ TYACSSTTNP
     TFSSNCTSGV TFTVPAQPSL DSVTPQQSTV NPSTSTPTAT SSVSPKSSTK TPVGKSQSMN
     TGSSTTRLSQ ANSVKISLIL FVVILAIASW YTTH
//