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Database: UniProt
Entry: A0A1H4DSV6_9BACT
LinkDB: A0A1H4DSV6_9BACT
Original site: A0A1H4DSV6_9BACT 
ID   A0A1H4DSV6_9BACT        Unreviewed;       726 AA.
AC   A0A1H4DSV6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:SEA75588.1};
GN   ORFNames=SAMN05444145_10616 {ECO:0000313|EMBL:SEA75588.1};
OS   Alistipes timonensis JC136.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1033731 {ECO:0000313|EMBL:SEA75588.1, ECO:0000313|Proteomes:UP000183253};
RN   [1] {ECO:0000313|EMBL:SEA75588.1, ECO:0000313|Proteomes:UP000183253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25383 {ECO:0000313|EMBL:SEA75588.1,
RC   ECO:0000313|Proteomes:UP000183253};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNRI01000006; SEA75588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4DSV6; -.
DR   STRING; 1033731.SAMN05444145_10616; -.
DR   Proteomes; UP000183253; 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:UP000183253}.
FT   DOMAIN          22..102
FT                   /note="Alpha-N-acetylglucosaminidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12971"
FT   DOMAIN          116..449
FT                   /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05089"
FT   DOMAIN          457..711
FT                   /note="Alpha-N-acetylglucosaminidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12972"
SQ   SEQUENCE   726 AA;  84832 MW;  5007E8B924F744CD CRC64;
     MFAAIPLLAV RSASASGTAE TQAAAALARR ILPRLGAGIR FVHVPSDRDR FVLEMHGDEL
     HISGNSAVSM AFGLNCYLRE YCRVTVTWYR RDKIDEPKRL PAVEGRVERE ARVGNRFFLN
     YCTYGYSLNW WQWDEWEHFI DWMALNGVTM ALATTGQEAV WQRVWRRFGL DDDTIRGYFT
     GPSYLPWHRM ANIDAWHGPL PQSWIDGQLE LQRRIIARER ELGIQPVFTS FTGHVPKALK
     TLFPDADIER LNPWTSFERP YNSYYLNPAE PLFNRIQQAY MQEQRRLFGE SSVYGVDPFN
     ELDPPNWDPE YLARAARLTY ESITQFDKDA VWLQMAWVFY HKRRDWTPER LKAYLCAVPD
     GKLLMLDYYC DKVELWRSTE SFYGQPFIWS YLGNFGGNTM LAGDVKDVSR KLDRAYAEAG
     RNFVGIGCTL EGLDVNPFMY EYVLDRAWTQ LYDDAGWIDR LADRHSGRID VHYRQAWRIL
     YDKIYCAPSG NRSAAVCARP NMKGRSKWSG PHLDYDNRDL LRVWEQLTLA RPERTASSRF
     DCVNIPRQCL ENYFGNLNER CIAACRGGDR ETVARLSARL LELLDDIDRL VAADAYFLLG
     KWIADARRMG ATPAEKDYFE RDARNILTTW GGRGYSLNDY ANRTWSGLVS DYYKERWRRF
     YDRLQSDGEP DEDALLQELQ DFEWEWVGRK GRFAERPRGD AFRLCRSLYT KYAAEIGRFY
     TEKSER
//
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