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Database: UniProt
Entry: A0A0W0XYX0_9GAMM
LinkDB: A0A0W0XYX0_9GAMM
Original site: A0A0W0XYX0_9GAMM 
ID   A0A0W0XYX0_9GAMM        Unreviewed;       380 AA.
AC   A0A0W0XYX0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=Lrub_0342 {ECO:0000313|EMBL:KTD49900.1};
OS   Legionella rubrilucens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=458 {ECO:0000313|EMBL:KTD49900.1, ECO:0000313|Proteomes:UP000054608};
RN   [1] {ECO:0000313|EMBL:KTD49900.1, ECO:0000313|Proteomes:UP000054608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD49900.1,
RC   ECO:0000313|Proteomes:UP000054608};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD49900.1}.
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DR   EMBL; LNYT01000004; KTD49900.1; -; Genomic_DNA.
DR   RefSeq; WP_058530471.1; NZ_LNYT01000004.1.
DR   AlphaFoldDB; A0A0W0XYX0; -.
DR   STRING; 458.Lrub_0342; -.
DR   PATRIC; fig|458.5.peg.352; -.
DR   OrthoDB; 9786661at2; -.
DR   Proteomes; UP000054608; 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; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054608};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..380
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006917052"
FT   DOMAIN          27..371
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   380 AA;  41775 MW;  58ADE98DBCCF04FB CRC64;
     MSYLASALAM VLSLFMVSES EASDSRLRDK IGQMLIVGFE GKTVGKHSPI LQAIAEENIG
     GVILFDYSDQ TETFNKNIES PKQVQRLNRA LQHAADKANR RHHRKPLPLL ISVDYEGGEV
     NRLNAKYGFP AIPSAEAFAR LNDAKAHQLA ETIAVTLSSN GFNLDFAPLI DVNVNPDNPV
     IGQLHRSFSA DPTVVAHYAG VVASHLRAHG LQCAYKHFPG HGSSTADSHV GFVDVSQTWK
     TMELRPYRQL LHQQSSCGMI MTAHIVNRQL DESGLPATLS HKVLTGLLRD KLKFDGVIVT
     DDMQMKAISD HYGLEKALTL AINAGADMIM FGNQLSDKPQ ETKALVDLIE AKVKAGEISE
     KRIDEAYRHI VAFKSSLKKD
//
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