ID   A0A1H8WYU8_9SPHI        Unreviewed;       758 AA.
AC   A0A1H8WYU8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:SEP32653.1};
GN   ORFNames=SAMN05428947_11125 {ECO:0000313|EMBL:SEP32653.1};
OS   Mucilaginibacter sp. OK283.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP32653.1, ECO:0000313|Proteomes:UP000199509};
RN   [1] {ECO:0000313|EMBL:SEP32653.1, ECO:0000313|Proteomes:UP000199509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK283 {ECO:0000313|EMBL:SEP32653.1,
RC   ECO:0000313|Proteomes:UP000199509};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FODR01000011; SEP32653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8WYU8; -.
DR   STRING; 1881049.SAMN05428947_11125; -.
DR   Proteomes; UP000199509; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate 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; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 1.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR007781; NAGLU.
DR   InterPro; IPR024732; NAGLU_C.
DR   InterPro; IPR024240; NAGLU_N.
DR   InterPro; IPR024733; NAGLU_tim-barrel.
DR   PANTHER; PTHR12872; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR   PANTHER; PTHR12872:SF1; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR   Pfam; PF05089; NAGLU; 1.
DR   Pfam; PF12972; NAGLU_C; 1.
DR   Pfam; PF12971; NAGLU_N; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..143
FT                   /note="Alpha-N-acetylglucosaminidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12971"
FT   DOMAIN          164..484
FT                   /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05089"
FT   DOMAIN          493..755
FT                   /note="Alpha-N-acetylglucosaminidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12972"
SQ   SEQUENCE   758 AA;  87161 MW;  824BB591FC525558 CRC64;
     MKTYATVCAC RNKRLRKFYA ATAPGCALFS ILILVSFEDV NPKNQYFYMR KLTFLLVLLL
     PIHLFAQQFE PVKALVKRRA PWLSDHIIFK TLKSPDSEIA QLQTVKNKLV ISASGPNAAA
     VGVNWYLKYY CHRSMSHMGD NLAPVFPIPA VGKKETVKAE AKYRYALNYC TYNYTMSFYS
     WADWERELDW MALNGVNTML TVEGMEAVWQ NTLRKIGYNE NEINNFIVGP AYTAWWLMGN
     IEGWGGPMPQ SQIDNRKLIQ QKMIKRMQEL GIEPVLQGFY GMVPSTLKNK SKAHIIDQGN
     WGAFKRPDIL DPTDPEFSRV AGIYYSEMQA LYGKNIHFFA GDPFHEGGKT DGIDLKKAGA
     SIQASMQSYY PGSVWVLQGW QDNPKQAMLD GLDKSKVLVQ ELFGEFTNNW EKRKAYDNTP
     FIWCSVNNFG ERPGVYGKLQ RFADEIYRAR ESTYSNYLKG VGIMPEGINN NPPDYDLMLE
     LGWRTEHVDT RTWINNYAKY RYGVNNAHTS NAWQGFLQTI YQSLPGYQEG AGESIFCARP
     ALKVKSISSW GTLTRNYDTV QFEKAVKEFA LAAPGLMNSA TYKIDLINMV RQVLSNKGTL
     VFNDLVTAYN NKDLPAFNKA SEKFLHMIKL TDDLLNTDGY FRLNTYLKQS IANGNTAEEK
     ANNLKNALMQ ITYWGENIRT EDNLHEYAYK EWAGLINSYY LPRWEIYFDY LRGNLQGKNA
     PEPDYFSWER KWVDENQKLN PEKPHRPLQE VVNQILSM
//