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Database: UniProt
Entry: A0A0E3ZZS9_9BACT
LinkDB: A0A0E3ZZS9_9BACT
Original site: A0A0E3ZZS9_9BACT 
ID   A0A0E3ZZS9_9BACT        Unreviewed;      1028 AA.
AC   A0A0E3ZZS9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=SD10_26020 {ECO:0000313|EMBL:AKD57843.1};
OS   Spirosoma radiotolerans.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD57843.1, ECO:0000313|Proteomes:UP000033054};
RN   [1] {ECO:0000313|EMBL:AKD57843.1, ECO:0000313|Proteomes:UP000033054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5A {ECO:0000313|EMBL:AKD57843.1,
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 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; CP010429; AKD57843.1; -; Genomic_DNA.
DR   RefSeq; WP_046578052.1; NZ_CP010429.1.
DR   AlphaFoldDB; A0A0E3ZZS9; -.
DR   STRING; 1379870.SD10_26020; -.
DR   KEGG; srd:SD10_26020; -.
DR   PATRIC; fig|1379870.5.peg.5625; -.
DR   HOGENOM; CLU_012120_0_0_10; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000033054; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AKD57843.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033054}.
FT   DOMAIN          94..408
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          640..1007
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   1028 AA;  113362 MW;  9235008EB3F3E67E CRC64;
     MRNIVVRPIL LVGLLLVSLL TAFGLMKPGR NFWAKLARTT AIRAAAKRTA AANANRLALA
     SYKFGPAARP VEVFAMSDSG EHWVDSVFHT LTPEQKIGQF FMVATFSNRH DNHYQYIDHL
     IQTNHIGGLI FFQGGPYRQA VLTNRYQAES KVPLLIGIDG EWGLGMRLDS TMDFPKQMSL
     GAIRDNEVIY RMGAEIGRQC QRLGIHINFA PVSDINSNPA NPVIGVRSFG ESKENVALKA
     SAYMRGLQGT HVIATAKHFP GHGDTNVDSH HTLPTVSRSS EQMREIDLYP FRKLIADSLM
     GVVTGHLHVP VMDNTPALAA TLSEKIVTEL LKKELGFRGL VFTDALNMGG ISRSPKAMDV
     NLRALMAGND ILLYPENVRE ATTNIMNAVQ QGVISQELID EKVKKILRAK YWAGLAQYKP
     INLAGLSTDL NSPEAKLLKQ ELCEQSVTVA DNKNSLLPLK HLDTLRLASV AIGAEPGNVF
     QKTLNQYAPF QTLAYPEKPV SEADLTNILA QVGDANTVVV SFHRMSESAL RKYGITKPSL
     DLITRLKQRG AKVIVTAFGS PYSLQQFTGA DALVCAYQEL EDMQRVVPQI LFGGLGSQGM
     LPVSIGDMKV GMGLTLGPEG RLSVGSPESV GMKSTVLNQI DAIAQGAVKN HVVPGCEILV
     ARKGKIVYSK NFGALTYSPN AEKVTDETLY DLASLTKVLA TLQSVMVLYD RKQIDLTQKA
     SFYLPELKNT NKQNITLLDL LWHQSGMVSF YPTTWDRTRL PGGGLKAEYY ASVHDSLHTL
     QIAPTLWGVP ALRDSVWKWV VQSPMSKKND EAGRPAFVYS DLNFLTLQKV VERVSKQPLD
     KFVTDNVYKP LGLHQLGFTP LQRLTNPKCA PTEQDTYYRN QLLVGTVHDQ MAAVQGGISG
     HAGLFGNAHD IATLLQMNLQ KGVYGDERIL QPMTVPYFTQ TLSNRSHRAL GWDKPNPESA
     SSVYMAQQVS PRSFGHTGFT GNVVWVDPDQ ELIFVFLSNR IYPTAGNNSI NTTKLRRRIH
     EVIYSAVQ
//
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