ID A0A1Q4X1R4_9PSEU Unreviewed; 581 AA.
AC A0A1Q4X1R4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=A6A25_12520 {ECO:0000313|EMBL:OKI16276.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI16276.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI16276.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI16276.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
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:OKI16276.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWLC01000056; OKI16276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4X1R4; -.
DR STRING; 1835005.A6A25_12520; -.
DR Proteomes; UP000186828; Unassembled WGS sequence.
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 PRINTS; PR00133; GLHYDRLASE3.
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|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000186828};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..581
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012547108"
FT DOMAIN 38..371
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 414..576
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 581 AA; 61416 MW; 2C6FF80FBA8EC64A CRC64;
MFNRRQVLVA VSALLVGSAP AMATDGDVVA DTLRRMSLEE KVGQLFVTYA YGAAVDASDP
ASVAANRRQH GVDNARQLIE KYHLGGIIYF AWSGNTANPG QVAELSNGIQ RVSSVPALVS
TDQEYGVVTR IGAPATLFPG NMALGAARDP GSAGTAALIA GRELRAMGVN QDFAPVADVN
VNALNPVIGV RSFAEDPELT AQLVEAQVRG YERGGVSATA KHFPGHGDTA VDSHTGLPVI
GHSVEEWERL DAPPFRRAIA AGIDSIMTAH IVVPALDPSG DPATLSRPII TGILRDRLGY
DGVVITDSLG MAGVRQKYGD DRVPVLALKA GVDQLLMPPS IDLAFNAVLT AVRTGELTER
RIDQSVRRIL RMKAKRGLFG GQFVDPAQLP RVVGTEQNRQ TAQRITDRTT TLVRNAHLPL
RTPPASVFTT GWGTTADPVP HRLATAVAKR SATTNALVTG ANPNQATIDR AVAGAAGADL
TIVATNKAWT DVGQQNLVKA LLATGKPVVV IAVRDPYDIA YFPDARTYLA TYSYTDISVE
SAVRVMYGEH APVGKLPVTI PVAGDPSTAL HPFGHGLTWE G
//
