ID A0A1I1M9K5_9SPHI Unreviewed; 613 AA.
AC A0A1I1M9K5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=SAMN05421747_1319 {ECO:0000313|EMBL:SFC82054.1};
OS Parapedobacter composti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=623281 {ECO:0000313|EMBL:SFC82054.1, ECO:0000313|Proteomes:UP000199577};
RN [1] {ECO:0000313|EMBL:SFC82054.1, ECO:0000313|Proteomes:UP000199577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22900 {ECO:0000313|EMBL:SFC82054.1,
RC ECO:0000313|Proteomes:UP000199577};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; FOLL01000031; SFC82054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1M9K5; -.
DR STRING; 623281.SAMN05421747_1319; -.
DR OrthoDB; 1006965at2; -.
DR Proteomes; UP000199577; Unassembled WGS sequence.
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; 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; PF13290; CHB_HEX_C_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199577};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..613
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011509556"
FT DOMAIN 27..153
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 157..498
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 330
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 613 AA; 69210 MW; 412BCD337FCDA742 CRC64;
MNRLAKLSVI IALLLSSGTQ AQEHTFSIIP QPLQLEPKQG GFLIRKTTTI QLDDNRPELR
ALAELLAQGL FERTGTRPRI TSGKGGSNAI ALQLVQDTLG DEGYRLTVGK GGITARAAKG
NGLFYAIQTI YQLVPADQTA SKPVTVPAVE IVDKPRFGWR GLMLDVGRYF YSVDYVKKFI
DYLAMHKMNT FHWHLVEDHG WRIEIKKYPR LTDVSAWRPS TNFQRGGYIN RNPHGGYYTQ
EDVKEVVAYA QSRYVTVIPE IELPGHVLSA LVAYPELSCS GGPFEIPEQW GIQKDIYCAG
KEEVFTFLEG VLSEVAELFP SEIIHIGGDE APKDRWKACP HCQKRIKDEG LKDEHELQSY
FITRIEKFLN GKGKRIIGWD EILEGGLAPN AAVMSWRGIK GGIEAARMHH PVVMSPTTHM
YLDYFQGEPY HEPNAIGGHL PLRKVYSFEP VPEELVGKER DFILGVQGNV WAEYIHSPDK
ADYMTYPRAA AVAEVGWSMP DRKDWEDFTR RMEAQYRRYD GVGINYARSA YQVYFEVEDN
VAGNVSKVSL KTDSYRPEIR YTTDGTEPTA SSTRYDGPFE VTEYTTVRAA TFKDGKRISP
VSIRSMVHFG QTD
//
