ID A0A2U2PI24_9SPHI Unreviewed; 728 AA.
AC A0A2U2PI24;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:PWG80912.1};
GN ORFNames=DDR33_09865 {ECO:0000313|EMBL:PWG80912.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG80912.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG80912.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG80912.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL Submitted (APR-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:PWG80912.1}.
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DR EMBL; QEAS01000007; PWG80912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2PI24; -.
DR OrthoDB; 179563at2; -.
DR Proteomes; UP000245647; 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:UP000245647}.
FT DOMAIN 38..116
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 130..476
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 485..719
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 728 AA; 83655 MW; 49C89027F274CDBF CRC64;
MDILSMYKKI ILFFILASWN GINVEARQVD VGSITASSRN VIRRTIGNRA DAIDLQVVPS
ENGTDVYEIE ARGGVLTVRG SSPSAICSGF YEYLRKACKS MVSWSGSNLH IPLKWPDYSK
VKVVSPYRYR YYLNVVTFGY TTPYWDWARW EKELDWMALH GVNLPLATVA SETIAARVWK
KLGLSNKETD AFFTGPAHLP WHRMGNLNKW DGPVPSDWHK DQLDLQHKIL KRMRELGMNP
VAPAFAGFVP EGFKKKHPEL HVNALKWGGF PAEYNAYVLS PGSPWFKTIG KMFVEEWEKE
FGKNTFYLSD SFNEMDVPVP KDHPEQKYPL LAGYGESIYN SIKAGNPDAV WVTQGWTFGY
QHKFWDQRSL QAMLSKVPDD RMLILDLANE YPEYVWKIPM VWKTHQGFYG KQWIYSFVPN
FGGKTPWTGV LSLYASGSAE ALKSPFSKNL VGFGSAPEGI ENNEVVYELL ADMGWKRDAV
DLDKWLDEYC RSRYGAYPDK MKLAWEQLRK SAYGSFGSYP RFLWQLVVPD TRRKGSVNSD
SLFMRSAENF LDCSEELKAS KLYQNDAIEI AMLYLGVRAD QWYSRALKAD AQNDQTVKRK
AGEKAVEILY QIDRLLESHP NNRLQTWVDY ARSHGKTEEE KNYYEANAKR LITTWGGVQN
DYAARIWSGL IRDYYIPRIQ KHLANAGFRR LDWEEKWIKT PGGSRVEPFD DPIQKAKELV
AAYGSIEL
//
