ID   A6LEX7_PARD8            Unreviewed;       773 AA.
AC   A6LEX7;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   OrderedLocusNames=BDI_2521 {ECO:0000313|EMBL:ABR44241.1};
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR44241.1, ECO:0000313|Proteomes:UP000000566};
RN   [1] {ECO:0000313|EMBL:ABR44241.1, ECO:0000313|Proteomes:UP000000566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC   {ECO:0000313|Proteomes:UP000000566};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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DR   EMBL; CP000140; ABR44241.1; -; Genomic_DNA.
DR   RefSeq; WP_009018328.1; NC_009615.1.
DR   AlphaFoldDB; A6LEX7; -.
DR   STRING; 435591.BDI_2521; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PaxDb; 435591-BDI_2521; -.
DR   KEGG; pdi:BDI_2521; -.
DR   PATRIC; fig|435591.13.peg.2504; -.
DR   eggNOG; COG3525; Bacteria.
DR   HOGENOM; CLU_007082_5_0_10; -.
DR   BioCyc; PDIS435591:G1G5A-2590-MONOMER; -.
DR   Proteomes; UP000000566; Chromosome.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06563; GH20_chitobiase-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR026876; Fn3_assoc_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF13287; Fn3_assoc; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABR44241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..773
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002698808"
FT   DOMAIN          30..157
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          160..509
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   DOMAIN          638..758
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   ACT_SITE        334
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   773 AA;  85807 MW;  8BB6A601A017F50F CRC64;
     MNSLSKLALV LTFCTGMIAC SGGKAVKGDY GVVPLPQEVT LTNGNPFVLS PSTKIFYPEG
     NDKMKKNAEF LASYIKEITG YELATATGQP GKGISLVIDQ SIQNPEGYQL TVSDNGIRIA
     GSTDAGVFYG IQTLRKSIPA TAQGMNVELP AATINDYPRF AYRGMMLDVS RHFFPVDSVK
     TYLDILALHN QNTFHWHLSD DQGWRIEIKK YPELTQIGSK RKETVIGHNS GTYDGKEYGG
     FYTQDQIRDV INYAAERHIT IIPEIDMPGH QLAALATYPE LGCTGGPYDV WGQWGVADDV
     ICAGNEKSMQ FLEDVLSEVI DLFPSEYIHV GGDECPKVRW EKCPKCQARI KAEGIKGDKK
     HSAEEYLQSY VISRMEKFVE SKGRHIIGWD EILEGGLAPN ATVMSWRGMD GGIEAAKQKH
     NVVMTPNTYV YLDYYQSADT DLEPDAIGGY LPLEKVYSFE PTAGISPEDQ KYVIGAQANL
     WTEYIPTFSQ VEYMIMPRID AVADIQWSDP SKKDYQTFLP RVARMTQLYD RLGYNYGKHI
     FDINASLTTN TENGTLDIAL TKLGEGDIYY TVDGSDPTIA SIKYEGPVQI NQDCEFKAIV
     VRPNGTSRIF SEDIFFNKAT MKPITLKEQP SKGYVFNGAQ VLVDGLRGGS NYKTGHWLGF
     QGKDLDATID LKEPTEIQKV SFNTNVVKGD WIMGASAVTV KVSDDGKNFK EVASKKIPEL
     TQNDKDGLYP QEISFAPVNA RYVEIIINSS KLPKWHGGAG SPAFLFVDEI EIL
//