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Database: UniProt
Entry: D7TM08_VITVI
LinkDB: D7TM08_VITVI
Original site: D7TM08_VITVI 
ID   D7TM08_VITVI            Unreviewed;       541 AA.
AC   D7TM08;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   OrderedLocusNames=VIT_13s0019g00040 {ECO:0000313|EMBL:CBI31745.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI31745.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN595998; CBI31745.3; -; Genomic_DNA.
DR   RefSeq; XP_002282535.1; XM_002282499.3.
DR   AlphaFoldDB; D7TM08; -.
DR   STRING; 29760.D7TM08; -.
DR   PaxDb; 29760-VIT_13s0019g00040-t01; -.
DR   EnsemblPlants; Vitvi13g00245_t001; Vitvi13g00245_P001; Vitvi13g00245.
DR   GeneID; 100251825; -.
DR   Gramene; Vitvi13g00245_t001; Vitvi13g00245_P001; Vitvi13g00245.
DR   KEGG; vvi:100251825; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   InParanoid; D7TM08; -.
DR   OMA; NYCVEPP; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000009183; Chromosome 13.
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:SF40; BETA-HEXOSAMINIDASE 1; 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:UP000009183};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..541
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003106328"
FT   DOMAIN          39..160
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          185..489
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        332
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   541 AA;  61530 MW;  87D0C08863B5680D CRC64;
     MAVPYHFSSF VFVFTLICAL GVSLGFNSTS DLDDSLVYLW PLPSEFTFGE DVLAVDPDLS
     LAVGGDGGNS DIVREAFLRY RGIIFKHSTR FSKFRGRSMY DISKIRIIVH SDSEMLQLGV
     DESYSLLVAK NDDHSIIGEA TIEANTVYGA LRGLETFSQL CAFDYGTKTV QVYNAPWYIQ
     DKPRFVYRGL MLDTSRHYLP IDVIKHVIES MSYAKLNVLH WHIIDEQSFP LEVPTYPKLW
     KGAYTKWERY TVEDAYDIVN FAKMRGINVM AEIDIPGHAE SWGTGYPDLW PSPSCREPLD
     VSKEFTFDMV SGILTDMRKI FPFELFHLGG DEVNTDCWNS TPHVQQWLQD HNMTPKEAYQ
     YFVLRAQEIA ISKNWAPVNW EETFNTFATN LNPRTVIHNW LGPGVCPKAV AKGFRCIYSN
     QGVWYLDHLD VPWDGFYNAE PLEGINSASE QELVLGGEVC MWSEVADTSN VLQTIWPRAA
     AAAERLWSKR EATSGKNITL TALPRLHYYR CLLTRRGVEA DPVTNKYARQ PPNGPGSCYE
     Q
//
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