ID A0A416G9D4_9BACE Unreviewed; 717 AA.
AC A0A416G9D4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:RHP61544.1};
GN ORFNames=DXA74_13335 {ECO:0000313|EMBL:RHP61544.1};
OS Bacteroides sp. OF04-15BH.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292281 {ECO:0000313|EMBL:RHP61544.1, ECO:0000313|Proteomes:UP000284249};
RN [1] {ECO:0000313|EMBL:RHP61544.1, ECO:0000313|Proteomes:UP000284249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OF04-15BH {ECO:0000313|EMBL:RHP61544.1,
RC ECO:0000313|Proteomes:UP000284249};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHP61544.1}.
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DR EMBL; QUEM01000034; RHP61544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416G9D4; -.
DR OrthoDB; 179563at2; -.
DR Proteomes; UP000284249; 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:UP000284249};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..717
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019527634"
FT DOMAIN 21..100
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 115..441
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 450..715
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 717 AA; 82692 MW; 6E8A70F032C25B6C CRC64;
MKKIKTLFLM AWTSSIAWAS PIDNLLERID EGASQKFITE EINSASKQDF FELDQKGQKV
VVRGNNPVSI ATGINWYLKY YAGIHLSWNN MKADLPEVLP PVTQVERHST DQVERYYLNY
CTHSYSMAFW GWERWEQEID WMALHGINLP LAVVGMEEVW YRVLDKLGYS DQEIGEFIAG
PGFQAWWLMN NLEGWGGPNP KNWYKDRVNL QKKILKRMRE LGIKPVLPGY SGMLPHDARE
HLGVNVSDPG TWCGYRRPAF LQPTDPNFER IAKLYYQELT RLYGKADYYS MDPFHEGGNV
AGVDLNAAGI AIWKAMKQTN KNAVWVAQAW QANPRPQLIG GIPKGDLIVL DLFSESRPQW
GDPNSTWKRE NGFDGHDWLY CMLLNYGGNV GLHGKMETVI RKFYQAKESR FGATLKGVGL
TMEGIENNPV MYELLCELPW RSTSFTKEQW LEGYVAARYG KKDERVLKAW TILSNSIYNC
PEKSTQQGTH ESLFCARPSL NAYQASSWSE MSDYYNPQDV IQAARLMVEA APAFQGNNNF
EYDLVDIVRQ AVAEKGRLVY PIVVSAYKSG EKELFNQAAE RFIRLIDMQD KLLATRPEFK
VGTWLQAARK LGHTEEEKNL YEWNARVQIT TWGNRTAADQ GGLRDYAHRE WNGLLRDFYK
MRWNTYFDIL RQRLDGKQVA DPDYYALEEP WTLQHNLYSS EPEGEAVKVA TEVFRNL
//