ID B7GNQ7_BIFLS Unreviewed; 651 AA.
AC B7GNQ7; E8MNY9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=Blon_2355 {ECO:0000313|EMBL:ACJ53413.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ53413.1, ECO:0000313|Proteomes:UP000001360};
RN [1] {ECO:0000313|EMBL:ACJ53413.1, ECO:0000313|Proteomes:UP000001360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]
RC {ECO:0000313|Proteomes:UP000001360};
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CP001095; ACJ53413.1; -; Genomic_DNA.
DR RefSeq; WP_012578580.1; NZ_JDTT01000072.1.
DR AlphaFoldDB; B7GNQ7; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR KEGG; bln:Blon_2355; -.
DR PATRIC; fig|391904.8.peg.2431; -.
DR Proteomes; UP000001360; 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; cd06565; GH20_GcnA-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACJ53413.1}.
FT DOMAIN 10..130
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 134..378
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 651 AA; 72784 MW; 4107C01C9E22E87F CRC64;
MVQEPTLEWH VIPEPTNVEP LVGTCSLPLS GTVVEQRGAD DAEAVFARQL VDDIKRVCGG
RWQVASGEVQ REVTLRTSPS LDDWSYVLEV SPDGVVITGS GFEGVRDGVQ TLRQIIRQIG
LTIPCMVIRD RPAFSTRGYY LDVTRGRVPS MAWLKSWVDR LCFYKYNQFQ LYIEHTFQFN
GLSEVWRGAD PLTSSDILEL DSYCAARGIE LVPSVSTFGH HYTALRTRQL RDLGEFPEDA
DRPFSLIERM THHTLNITDE RSYEFSTSLI DELMPLFRSR KFNICADETF DLGKGRSKQE
SAKRGVGAMY ADFVERLCRH VDDRGHDVMV WADVALEHPE IIDTLPKNIT WLNWQYEPNV
DDGTTAALAD AGATQMVCPA VWCWNALIPR IDDAWNNITR MARHGRAHDV SGMLVTDWGD
FGHVNDPRMS VPGMIFGAQQ SWNPDAELSE VDMLSRISTI EYGDHTGSVV GALRGASAKG
GFSWSDLVTY LELDDGRGGC NTEIVRVMGC LEAYRNDLPQ SGQARLADAR VSMLRTLRDS
ILAGRELNGK LDDAAKDITQ LLRVAGDPSS AAVWSLAIDG QRLLNRVGLA LLAAHGVVRQ
DEAGIDAAKL ADELECWTEQ YSRLWHEVSR QSELARIQHV VWRAADVLRS I
//
