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Database: UniProt
Entry: K1QJV3_CRAGI
LinkDB: K1QJV3_CRAGI
Original site: K1QJV3_CRAGI 
ID   K1QJV3_CRAGI            Unreviewed;       884 AA.
AC   K1QJV3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00030512};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN   ORFNames=CGI_10002999 {ECO:0000313|EMBL:EKC21981.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC21981.1};
RN   [1] {ECO:0000313|EMBL:EKC21981.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC21981.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
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}.
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DR   EMBL; JH815813; EKC21981.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1QJV3; -.
DR   HOGENOM; CLU_007082_4_1_1; -.
DR   InParanoid; K1QJV3; -.
DR   OMA; SANCEIP; -.
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:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02847; E_set_Chitobiase_C; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004866; CHB/HEX_N_dom.
DR   InterPro; IPR004867; CHB_C_dom.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF03173; CHB_HEX; 1.
DR   Pfam; PF03174; CHB_HEX_C; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SMART; SM01081; CHB_HEX; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          67..225
FT                   /note="Chitobiase/beta-hexosaminidases N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01081"
FT   ACT_SITE        572
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   884 AA;  101165 MW;  996170F5BFFF2B11 CRC64;
     MPLTSLHFNH SLQFCESFLI EEFKFPVPPT KTSPQEKGKF SPEEIEVKRK KSLSKQESQV
     YVNYMADNFV INFTVIQNSA RTCIKKFSIY NAGQRNIPSF FWAIYFYDNG KVGHNSFPYP
     RGLPVDNSEL LIFHEAGNLY RLSPTEKFSP YINSRDTIEV PYESYGPHVS RHYSFPNWFV
     SCDICSPRVL KSTAGEDLSF VETFSKPQQL KRNSRDLYRA FTAKDRFSRN SAAAKAPKPS
     VHSVIPTPLR VDAGGEESLV VTPSDWVVST KDFVEEASLL AEKLHLKIAK SATSKVITFS
     QGKVTLPKNS SLSISEAYHI YINPSKNTIE VTANEASGAF YAAQTLLSLT EKDRSDSSKE
     KGHRFPGMNI TDAPRFEYRG LMLDVSRNFV QKATVLKLLD LMATYKVNKF HFHLTDDDAW
     RLEIPEFPEL TKYASNRCLD PSHEVCLPPS LGSGPFVNTS GSGFYTVNDY KEILRYAKSR
     HIEVIPEIDV PGHARSAIQA MELRYRRTKN SMYRLIDPDD RSRYLSAQSY TDDAVNPCVD
     GTYQFFKVIL RNLQELHKDI QPLTFYMLGG DEVAGGAWEK SPACADLKQK HELRDYHDLK
     KFFFKRMMEE LRQEDLTFGL WGDAVLDKSL NPNPLEEGTK GKVYTYSWSN VWEWKRGSLA
     YKLANAGYKP YEPDFEERGL YWATRCLDSR TAFSFVPDHL YWNRGRTQDG GEMTDEILCT
     GGCPPLTQPQ NIRGIQADLW TETIRTPQHL HYMLFPRFLA FAERAWHKAS WEDLTDVAQR
     DKEQQKDWER FAAIVGKEEL ERLESEGVEY RLDPPGARFS NSILEINTIF PGLPTEYSLN
     QGASWEKYNP KITTNLSNAG KILVRSSSFD GKRKSRVVSV ENSN
//
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