ID A0A0M8VEI2_9ACTN Unreviewed; 519 AA.
AC A0A0M8VEI2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:KOV63860.1};
GN ORFNames=ADL00_23050 {ECO:0000313|EMBL:KOV63860.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV63860.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV63860.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV63860.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:KOV63860.1}.
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DR EMBL; LGDU01000242; KOV63860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8VEI2; -.
DR PATRIC; fig|1519489.3.peg.5172; -.
DR Proteomes; UP000037758; 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; cd06564; GH20_DspB_LnbB-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; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 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:UP000037758}.
FT DOMAIN 51..168
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 175..480
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 23..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 519 AA; 55634 MW; EFAB8DF183672F8C CRC64;
MITVAVTAVV AVALSLGLWA GEDGGPTVSG RGTAAEPTPS PTRSYPLSSA PNTIPAVRGH
TPERGPGWRP ARGQRVVVSD AGLADEGRLI AGELGMSYGG DRDDTRAGDL RLALGRGGST
NPESYTLTVR GGQVTISAPA DAGVFYGTRT LKQTVRDGAT APEGVMRDEP AKPQRGLMLD
IARKHFTAGW IEDRVRELGD LKFNQLGLHF SDDQGFRIES ASHPEIVSAQ HLTKAEVTSI
VRLARSRHIT VVPEIDSPGH LGAVIAAHPD LQLRNAQGVP ARGAVDISKP AAAEIVDDLL
DEYAGLFPGD QWHLGGDEYQ ALMVSDPQAS YPQLAAAARR AYGSGGTVAD LATGWLNDRA
ATVRANGRVP RAWNDGFYAG TSVQPDKDIK VAYWTGKEIG ARVPAEYLAA GRQVVNYNDE
FLYYVLGEPQ TFVYPTGQRI YEQWTPRVLR GTEAVPAQYD AQILGGSLAV WCDLANSQTQ
DQVAAGIRMP LRATVQKLWD PTRPELTWAE FGKLADQLG
//