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Database: UniProt
Entry: W0HQ58_9GAMM
LinkDB: W0HQ58_9GAMM
Original site: W0HQ58_9GAMM 
ID   W0HQ58_9GAMM            Unreviewed;       643 AA.
AC   W0HQ58;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=Sant_0881 {ECO:0000313|EMBL:AHF75961.1};
OS   Sodalis praecaptivus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF75961.1, ECO:0000313|Proteomes:UP000019028};
RN   [1] {ECO:0000313|EMBL:AHF75961.1, ECO:0000313|Proteomes:UP000019028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 {ECO:0000313|EMBL:AHF75961.1,
RC   ECO:0000313|Proteomes:UP000019028};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(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, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP006569; AHF75961.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0HQ58; -.
DR   KEGG; sod:Sant_0881; -.
DR   PATRIC; fig|1239307.3.peg.946; -.
DR   HOGENOM; CLU_008392_5_2_6; -.
DR   Proteomes; UP000019028; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
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; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019028}.
FT   DOMAIN          57..414
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          450..628
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
SQ   SEQUENCE   643 AA;  70151 MW;  522602CC0CC17AF2 CRC64;
     MMTAPCLPRA REHMMNTIPP TRVTGVAAVT TQTPRANALG QALTRADNSQ SVLAGMTLRE
     KIGQKIMLDF RYWGRDSASG AARDTVALNA CIENILRDYH IGGVILFANN LKDADQIRRL
     TGQLAAVPQT HGIGLLIGTD NEGGNVFRLP RGDYTAFAGN MALGALYEGH GESALPYLQG
     KIMAQELCSL GLNLNFAPVV DVNSNQANPV INVRAFGDCP AQVDRLARQM VKGSAQIVTC
     YKHFPGHGDT HTDSHLNLPR VDRNREQAFA VDLAPYIAAI ADNDAPDMIM TAHIQYPALD
     DSLITRLDGE DIIVPATLSR RIQHHLLRQE MGYRGVTITD ALDMKAISDH FDPRDVVKRV
     FNAGVDIALM PVSVQAADEE DKLRELIDYI VAQVERGEID CEEIDVSVAR ILTLKRAKNI
     LAGQAASAAI GETERRLAKE VESAIADQSI TLLQNHQLLP LRDVSRRIAI FTPWGEQGHA
     VRQVLQQKGF HDVSSHKIDE IAWQAQRQEI DRCDIVIVGS QAVGVSPVEN NGQASGANGT
     GDTAHIAAII DYAHRQQKKI VLLLMRSPYD IIHFDGKTDA IVATYAYYGL DNGVRRGESL
     FAAARALVGD LKPSGKLPVN IYNVDPQGAI TDIRYPRGFG LNG
//
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