HEXB_PSEO7
ID HEXB_PSEO7 Reviewed; 773 AA.
AC P49007;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Beta-hexosaminidase B;
DE EC=3.2.1.52;
DE AltName: Full=Beta-GlcNAcase;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE Short=Beta-NAHase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE Flags: Precursor;
GN Name=nag096;
OS Pseudoalteromonas piscicida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O-7;
RX PubMed=7574618; DOI=10.1128/aem.61.2.804-806.1995;
RA Tsujibo H., Fujimoto K., Tanno H., Miyamoto K., Kimura Y., Imada C.,
RA Okami Y., Inamori Y.;
RT "Molecular cloning of the gene which encodes beta-N-acetylglucosaminidase
RT from a marine bacterium, Alteromonas sp. strain O-7.";
RL Appl. Environ. Microbiol. 61:804-806(1995).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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; D29665; BAA06136.1; -; Genomic_DNA.
DR AlphaFoldDB; P49007; -.
DR SMR; P49007; -.
DR STRING; 43662.TW75_19265; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PRIDE; P49007; -.
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; -; 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; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF03173; CHB_HEX; 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; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..773
FT /note="Beta-hexosaminidase B"
FT /id="PRO_0000012015"
FT ACT_SITE 531
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT DISULFID 46..53
FT /evidence="ECO:0000250"
FT DISULFID 389..397
FT /evidence="ECO:0000250"
FT DISULFID 496..542
FT /evidence="ECO:0000250"
SQ SEQUENCE 773 AA; 86760 MW; DBB379885E004642 CRC64;
MKFNRLMALL FGVSSPLYAL DQTAVNWLGQ NLDVKYTLLD TKPTTCPKAQ QKCYYSELSF
SVRKENTKAN NDFAIFFSQL MPIYHVEGDN FAITHINGDI HKITPAAGFS GFSSAPTTVR
FYTKDSQVTR SEVYAKLCCE RTRSLKLTPQ VIKSTQTQRD NDTGLDCNLN LTPFVTLNQL
QTSSKDDTPW MGSEYLYQHQ VKPTLDAAIG LIPKPKQLTV LSDKRLNLAA GINLQLSGIS
ADAIAMAQQR LNTLGVKSTK EGLVVNVAVK PNKQSSPHYQ LTVAENNISI QGNNSAAAFY
ALQSLAGLLD INDLRIPMVD IIDTPRYDFR GLHVDVARNF RSKAFILQTI EQMAAYKLNK
LHLHLADDEG WRLAIDGLDE LTSVGAYRCF DLTETRCLLP QLGAGNDKNA QVNGFYSAED
YIEILRYAKA HHIEVLPSLD MPGHSRAAII AMEARYKKLM AQGKPEDAQK YRLVETADKT
RYSSIQHYND NTLNVCIANT YTFIDKVLSE VKVLHDRAGV PLNTYHIGAD ETAVLWLESP
ACKKLQASVK DFTNFNGYFI ERVAKLLDKK GIQVAGWSDG LGDVRAANMP ANIQSNGLGD
IKRKRAPVAH RFANQGWQVV LSSPDVTYFD FPYQSHPEER GNHWASRAIE SKKMFEFMPD
NLPAHAEIWK NTNNHAYIAN DSDSSLNKGV QFAGLQGHLW SEMLRSDAQA EYMLYPRLLA
LAERAWHHAE WELPYQAGRI YSQSSGYFTA KLQAQREADW QRFVAILGNS RTT