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}.
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; 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
//