ID C3QX47_9BACE Unreviewed; 845 AA.
AC C3QX47;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=BSCG_03459 {ECO:0000313|EMBL:EEO56531.1};
OS Bacteroides sp. 2_2_4.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO56531.1};
RN [1] {ECO:0000313|EMBL:EEO56531.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_2_4 {ECO:0000313|EMBL:EEO56531.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; EQ973361; EEO56531.1; -; Genomic_DNA.
DR AlphaFoldDB; C3QX47; -.
DR HOGENOM; CLU_007082_4_1_10; -.
DR Proteomes; UP000003969; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEO56531.1}.
FT DOMAIN 40..190
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 525
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 845 AA; 95097 MW; 9FE3A53EB031218E CRC64;
MIYRKTGKPM RNMLYIIWGS LCLLLVISGC KSTDGAKAPV SLTWKMGAVE VQPGYYENSF
VLKNISDVPL EKDWIIYYSQ LPREILQEES APVKVEVVNA NFFRMYPAEN FQPLAPGDSL
TVKFCCTNGL KKMSHAPEGT YWVSQSGSKQ GIPLPVGLTI QPLKGMETED WYPAPDKIYA
SNLALETTAQ LQQTDIFPSV KEAVPATGKE GFAIENKVKL TFHPDFANEA ELLKEKLATI
HGLEVVSEAP VTVHLDYLPE RETAVNGEYY RIDTGNGLIN ISASTSHGIF NGTQTLLSLL
KGQEKPFRLG ALSIRDYPDL PYRGQMLDIA RNFTTVEHLK KLVDVISSYK LNVLHFHFSD
DEGWRLEIPG LEELTSVGAR RGHTTDELEC LYPGYDGNYD PSAATSGNGY YTREEFIDLL
RYAAQRHVRV IPEIESPGHA RAAIVSMKAR YHKYVNTAPE KANEYLLSDA QDTSRYVSAQ
SYTDNVMNVA LPSTYRFMEK VIRELIAMYE EAEVPLTTIH LGGDEVPEGV WMGSPVCRTF
MDENGMTSAY ELSEYYITKM ADYLQQHHLQ FSGWQEVALG HPETTDRHLN QLAAGVYCWN
TVPEWEADEI PYQIANKGYP VILCNVNNFY LDLAYDAHPY ERGLSWAGYV DESKGFSMLP
YSIYRSSRTD MAGNPVDPDI AGKGKTTLTA SGKEHIQGVQ AQLFAETIRD FEWVEYYTFP
KILGLVERGW NAFPAWSTLT GEKERQAFNK ELGLFYSKVS EKEMPHWASR SINFRLPHPG
LCIKEGQLHA STPIRGGEIR YTTDGTEPTL RSELWKAPVA CDASVVKAKL FYLNKESVTS
TLKVD
//
