ID   A0A1I2THX7_9BACT        Unreviewed;       742 AA.
AC   A0A1I2THX7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:SFG64478.1};
GN   ORFNames=SAMN05216383_12515 {ECO:0000313|EMBL:SFG64478.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFG64478.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOOW01000025; SFG64478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2THX7; -.
DR   STRING; 1855325.SAMN05216383_12515; -.
DR   OrthoDB; 179563at2; -.
DR   Proteomes; UP000198560; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..742
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011796077"
FT   DOMAIN          30..108
FT                   /note="Alpha-N-acetylglucosaminidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12971"
FT   DOMAIN          123..456
FT                   /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05089"
FT   DOMAIN          466..730
FT                   /note="Alpha-N-acetylglucosaminidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12972"
SQ   SEQUENCE   742 AA;  86082 MW;  E9C31D189CFD8572 CRC64;
     MRKFVLVFAL FMGSLTASFA TPGKNGDVMA ARGLVRRLLP AYEKSFVFQT LKSDGDVFRL
     ESKGNKVVIS GNNANSMSVG LNHYLKYYCK VDVGWFSHDG ITMPAVLPKV PKAETVKARV
     KNRFFLNYCT FGYTMPWWDW QEWEHFIDWM ALNGVNLPLA ITGQESIWYK VWTELGLTDE
     EVRSYFTGPA HLPWHRMLNI DSWGGPLPKS WLDGQLKLQQ RITAREREFN MRPVLPAFAG
     HVPHALLRLF PKAKITKLGA WAGYPDQYAC SFLDPMDSLF LEVQKKFITT EDEMYGTDHI
     YGVDLFNELT PPSYEPSYLS RVSRQVYESL RLADPEAVWL QMTWLFWNER KDWTNDRIKP
     YITSYPKDKS LLLDYYCERQ EIWQRTDKYF GVPYIWCYLG NFGGNTMLVG DFKEINKRLE
     NTFQNGGDNF TGIGSTLEGF DCNPYVYEYV FEKAWDFGLH KDVKKWAAAL ADQRVGKIDN
     DAREAWRILV DSIYVAPSTP GQCPLINIRP TFGKYRTYYA NPRIKYDNQN LLRIADLLLR
     VNSNTAAYKF DVTNIVRQLL SNYYLTVFKQ YEDAYNRRDR QVMGRLQTEM LGVINDVDRL
     VGTQSYFLTG KWIADARKWG GDSLREARYY EQNARNLITT WSDKDQLLND YASRTWAGLT
     KTFYGKRWSM FFDAVNGALD EGKAFDEDRF AVYRDAVTTF ERYWWQACVG SFSAKPVGDS
     RQVASELVAK YRGHILNGPL SD
//