ID A0A0E3ZVU9_9BACT Unreviewed; 849 AA.
AC A0A0E3ZVU9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SD10_16755 {ECO:0000313|EMBL:AKD56305.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD56305.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD56305.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD56305.1,
RC ECO:0000313|Proteomes:UP000033054};
RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT isolated from gamma ray-irradiated soil.";
RL Curr. Microbiol. 69:286-291(2014).
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; CP010429; AKD56305.1; -; Genomic_DNA.
DR RefSeq; WP_046575259.1; NZ_CP010429.1.
DR AlphaFoldDB; A0A0E3ZVU9; -.
DR STRING; 1379870.SD10_16755; -.
DR KEGG; srd:SD10_16755; -.
DR PATRIC; fig|1379870.5.peg.3636; -.
DR HOGENOM; CLU_007082_4_1_10; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000033054; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033054};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..849
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002417325"
FT DOMAIN 35..195
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 520
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 849 AA; 94131 MW; 67ABE8F0379A893D CRC64;
MRSYSFLLLL FGLPFFINCS QTNTRETPTS TNASKPLTIT LELADNNYQN QGRSRSVLTL
TNTGSEDLPA TGWKLFFNGG NPTSLDASVA QVKLFNGDLH YISPGPKFSK LEPGKSTTIQ
VLAGKIRNKT DFPVGFYLVL DKNPEQAYPV DVAIKSGTIY EKSDRLLAEK IFDQNEKIKA
IPDDKLPKIF PTPVSYQEKG TPFLLDNQVV IVTDKAFDRE ADYLANSLKT VIGKKPAVQT
NGNGKTITLR KNPSLAAEGY ALHIGSDGVV LTASSGAGIF YGIQSLQTLL PAAALSGKAG
SVSLPGLDAT DAPRFPYRAF MMDMARNFQP KSEVLKVLDA MALYKLNTFH FHFSEDEGWR
VEMPSLPELT AVGAKRAHTT DPTKNLIPSY GSGPDLSNPS GTGFYSKADF VEILKYARDR
HIVVIPEIES PGHARAAIKA MNARYQRFMK AGNKTEAERY LLQDVADKSV YRSVQGWDDN
VIDVSLPSAY TFLERVVDDL RGMYKEAGAP LQTIHFGGDE VPGGVWEKSP SVQKLIASNP
SVKNTDDLWY YYFGKVNQLL KSRQLFLSGW EEIGLKKVKQ NGRVKWVPNE TFAGENFRVN
VWKNSPGSGA EDLAYRMANA GYKVILTGVT HMYLDLAYNQ LSEEPGQYWG GYVDIDKPFY
FIPYDYLRNL KDDNTGNRIN PSLIKSREVL TAKGKANIVG IEAPLWSETN RNPQQFEYKM
FPKLLAVAER AWAKDPAWAK ETNEAKSEQL YDQAWSEFIS QVGKRELPRL DVYAGGYEYR
IPPVGAKVIN GKVAANVQFP GLTIRYTMDG TEPTAQSPVY TEPVASSGPV KFKVFNAVGR
SGQTVTISK
//
