ID Q9ZN69_9ENTR Unreviewed; 885 AA.
AC Q9ZN69;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 93.
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 Name=nag1 {ECO:0000313|EMBL:BAA74506.1};
OS Enterobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=42895 {ECO:0000313|EMBL:BAA74506.1};
RN [1] {ECO:0000313|EMBL:BAA74506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G-1 {ECO:0000313|EMBL:BAA74506.1};
RX PubMed=10478453; DOI=10.1271/bbb.63.1261;
RA Matsuo Y., Kurita M., Park J.K., Tanaka K., Nakagawa T., Kawamukai M.,
RA Matsuda H.;
RT "Purification, characterization and gene analysis of N-
RT acetylglucosaminidase from Enterobacter sp. G-1.";
RL Biosci. Biotechnol. Biochem. 63:1261-1268(1999).
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; AB022786; BAA74506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZN69; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
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 CDD; cd06569; GH20_Sm-chitobiase-like; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..885
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004337544"
FT DOMAIN 36..197
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 885 AA; 98616 MW; CCCA7B01763034F1 CRC64;
MNAFKLSALA ALTATMGFLG GMGSAMADQQ LVDQLSQLKL NVKMLDNRAG ENGVDCAALG
ADWASCNRVL FTLSNDGQAI DGKDWIIYFH SPRQTLRVDN DQFKIAHLTG DLYKLEPTAK
FSGFPAGKAV EIPVVAEYWQ LFRNDFLPRW YATSGDAKPK MLANTDTENL DQFVAPFTGD
QWKRTKDDKN ILMTPASRFV SNADLQTLPA GALRGQIVPT PMQVKVHEQD ADLRNGVSPD
LSTLDKPAAD VVNQRFALLG VPVQANGYPI KTDIQPGKFK GAMAVPGAYE LKIGKKEARV
IGFDQAGVFY GLQSILSLVP TDGSGKIATL DASDAPRFQY RGIFLDVARN FHKKDAALRL
LDQMAAYKLN KFHFHLSDDE SWRIEIPGLP ELTEVGGQRC HDLSETSCLL PQYGQGPDVY
GGFFTRQDYI DIIKYAQARQ IEVIPEIDMP AHARAAVVSM EARYKKLHAA GKEQEANEFR
LVDPTDTSNT TSVQFFNRQS YLNPCLDSSQ RFVDKVIGEI AQMHKEAGQP IKTWHFGGDE
AKNIRLGAGY TDKAKPEPGK GIIDQSNEDK PWAKSQVCQV MIKEGKVADM EHLPSYFGQE
VSKLVKAHGI DRMQAWQDGL KDAESSKAFA TSRVGVNFWD TLYWGGFDSV NDWANKGYEV
VVSNPDYVYM DFPYEVNPDE RGYYWGTRFS DKRKVFSFAP DNMPQNAETS VDRDGNHFNA
KSDKPWPGAY GLSAQLWSET QRTDPQMEYM IFPRALSVAE RAWHRAGWEQ DYRAGREYKG
GETHFVDTKT LEKDWLRFAN ILGQRELAKL DKGGVAYRLP VPGARVAGGK LEANIALPGL
GIEYSTDGGK QWQRYDAKAK PAVSGEVQVR SVSPDGKRYS RAEKV
//
