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Database: UniProt
Entry: T0J1J3_9SPHN
LinkDB: T0J1J3_9SPHN
Original site: T0J1J3_9SPHN 
ID   T0J1J3_9SPHN            Unreviewed;       336 AA.
AC   T0J1J3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=L284_10335 {ECO:0000313|EMBL:EQB15799.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB15799.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB15799.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB15799.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQB15799.1}.
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DR   EMBL; ATHL01000075; EQB15799.1; -; Genomic_DNA.
DR   RefSeq; WP_021233916.1; NZ_ATHL01000075.1.
DR   AlphaFoldDB; T0J1J3; -.
DR   PATRIC; fig|1096930.3.peg.2046; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9786661at2; -.
DR   Proteomes; UP000015527; Unassembled WGS sequence.
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; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
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; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015527}.
FT   DOMAIN          15..287
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   336 AA;  36274 MW;  C96884BE4A825DA8 CRC64;
     MTPAIFGLSG LTLSADERAF FRDADPAGYI LFGRNVQDRE QLRALTDELR AIHGRDRLYI
     TIDQEGGRVA RMKPPVWCAY PPGEVFDKLY DLAPASAIEA ARDNAEALGM DLAEVGVTAD
     CHPPLDLRHT GAHDIVGDRS FGGDPMRVAA LGRATLQGLA RAGIVGCVKH IPGHGRAMAD
     SHKELPTVEA SEAELERDIQ PFRTLKDVPF GMTAHVRYTA WDAENPATLS PFVVREIIRK
     RIGFTGLLMS DDLDMQALSG SVPELAERAI TAGCDLALNC WAKMDDMIGI AQRVPGMRAE
     TAEKLDLALA SVTGTRATGT HAELLARRDA LLALAA
//
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