ID A0A1H4XFE0_9PSEU Unreviewed; 622 AA.
AC A0A1H4XFE0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Hyaluronoglucosaminidase {ECO:0000313|EMBL:SED04297.1};
GN ORFNames=SAMN04489727_6145 {ECO:0000313|EMBL:SED04297.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SED04297.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SED04297.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SED04297.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNSO01000004; SED04297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4XFE0; -.
DR STRING; 208445.SAMN04489727_6145; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000199622; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..622
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011771319"
FT DOMAIN 32..151
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 157..468
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 66255 MW; 00DD9640BC2F957D CRC64;
MTARRRALFA AAVTVAATLT AAGPATASGA LPPVSPTPQQ ISRTSADVPL PSSVALVTEP
GTDPAARELL TSLLRGHGVT VGGRGLVIRL GSTGEDIPEQ AEGYALSVSR AGITIGGRDG
AGQYYGVQTL RQLVARSGRG WVVRGATVRD WPDMALRGSI EGFYGPPWTT ADRLRQLAFL
GEVKANTYVY SAKDDTYLRA RWRDPYPAGE LATLGQLVRA ATAHHVDFTY ALSPGVSICF
SSAADVAAVM AKFQAVYDLG VRSFSLPFDD ISYTRWNCAA DQAAFGAPGQ AAAGTAQVSL
LNTITEDFVR THDGVRPLQT VPTEYSDLKD SPYKTELREH LDPSVVVQWT GTDVVPPSVT
TDEAAQVSTV YGRKVFLWDN YPVNDYEQSA GRLLLAPYAQ RQAGLSRYLN GIVANPMNQE
AASEVAEFGA ADFAWNDAGY APERSWPQAL ARLAGGDPRA TAALTVFADL EHLAPTFGPT
AWQPQAPVLA AKTAAFWPRW TAGDHRALDD LRAYAVRIRD AAAVIRAGRV ERAFVTEAGP
WLDAAALWGA ATVTRLDALS ATARGDRGQA ERLTAAADTL VTRAQAVKTG NTNRWGIRQA
LVGDGVLDTF LVRARAATVG QS
//
