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Database: UniProt
Entry: U5D4A7_AMBTC
LinkDB: U5D4A7_AMBTC
Original site: U5D4A7_AMBTC 
ID   U5D4A7_AMBTC            Unreviewed;       575 AA.
AC   U5D4A7;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=AMTR_s00068p00123470 {ECO:0000313|EMBL:ERN20446.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN20446.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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; KI392059; ERN20446.1; -; Genomic_DNA.
DR   RefSeq; XP_006858979.1; XM_006858917.2.
DR   AlphaFoldDB; U5D4A7; -.
DR   STRING; 13333.U5D4A7; -.
DR   EnsemblPlants; ERN20446; ERN20446; AMTR_s00068p00123470.
DR   GeneID; 18448862; -.
DR   Gramene; ERN20446; ERN20446; AMTR_s00068p00123470.
DR   KEGG; atr:18448862; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   OMA; GHDVVMC; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IBA:GO_Central.
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   GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
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:SF26; BETA-HEXOSAMINIDASE 2; 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   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..575
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004658627"
FT   DOMAIN          37..154
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          174..525
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        337
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   575 AA;  63615 MW;  E7AB05711EFBA867 CRC64;
     MNLHYIPNAL CSLSSLILLL FISSIPTSIA QPPQVLVWPK PRNLTWTPPY SSILLSPTFT
     ISYSGSNPYL QNAVSRYLRL ILAEKYTPVR PIPSNLTAST QPLQTLTLSV NDETPPLQHG
     VDESYSLSIP NGTAVLWSAT VWGAMRGLET VSQLVWGDPA RLPVGLEIWD SPLFEHRGVM
     LDTSRNYYGM REILRTIGAM SENKMNLFHW HITDSHSFPI VLPSVPELAE KGSYGAGMQY
     SAEEVRGIVE FGMSRGVRVV PEIDSPGHTG SWAAAYPEIV ACANMFWSPP GKDPLAAEPG
     TGHLNPLHPN TYPLLRNVLR DLAALFPDSF LHAGADEVIP GCWKADPKIQ AFLASGGTLS
     QLLETHVNAT QPYIESLNRT AIYWEDVLLD STINVKPELL SKETTILQSW NNGPNNTKLI
     TSMGYRAIVS SSAFYYLDCG HGDFLGNDSS YDKMGDEGNG GSWCGPFKTW QRIYDYDITY
     GLTAEEAKLV LGGEVALWSE QADGTVLDPR LWPRTAAFAE AMWSGNRDET GIKRYAEATD
     RLNEWRYRMV ARGVGAEPIQ PLWCLKNPGM CNLSQ
//
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