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Database: UniProt
Entry: A0A095ST78_9FLAO
LinkDB: A0A095ST78_9FLAO
Original site: A0A095ST78_9FLAO 
ID   A0A095ST78_9FLAO        Unreviewed;       996 AA.
AC   A0A095ST78;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=LG45_12155 {ECO:0000313|EMBL:KGD67861.1};
OS   Flavobacterium aquatile LMG 4008 = ATCC 11947.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1453498 {ECO:0000313|EMBL:KGD67861.1, ECO:0000313|Proteomes:UP000029554};
RN   [1] {ECO:0000313|EMBL:KGD67861.1, ECO:0000313|Proteomes:UP000029554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 4008 {ECO:0000313|EMBL:KGD67861.1,
RC   ECO:0000313|Proteomes:UP000029554};
RA   Gale A.N., Pipes S.E., Newman J.D.;
RT   "Whole Genome Shotgun of Flavobacterium aquatile LMG 4008.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001231};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KGD67861.1}.
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DR   EMBL; JRHH01000004; KGD67861.1; -; Genomic_DNA.
DR   RefSeq; WP_035127443.1; NZ_MUGQ01000007.1.
DR   AlphaFoldDB; A0A095ST78; -.
DR   STRING; 1453498.LG45_12155; -.
DR   eggNOG; COG1472; Bacteria.
DR   eggNOG; COG1680; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000029554; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029554};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..996
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001917963"
FT   DOMAIN          74..387
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          427..580
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   DOMAIN          619..972
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   996 AA;  112298 MW;  9A81268B00736DFE CRC64;
     MKNLIKLFSF LLLITFLTNC SSSKDKTSKK LKKPNSVVED IYVPHLKSDR KTFFKGSLAE
     DKWVDSVYNQ MPFNEKVGQL FMVAAYSNKD SVHVNGLDKL ISDYKIGGLI FFQGGPVRQA
     KLTNRFQSKS KLPLFIGIDA EWGLSMRLDS TYKFPWNSTL GAIRDLKLIE KMGEQLGKES
     KRMGIHFNFA PVLDINTNPK NPIIGHRSFG EDKVNVTDRA IALMTGVQNQ GVFATGKHFP
     GHGDTATDSH YALPLVNFSR ERLENVELYP YKRMFDEGLE SVMVAHLNVP SLEARPKVPT
     SLSYNVVTDL LKKEMAFDGL IFTDALNMKA ASNFKKPGDI DLEALLAGND ILLFAENVPV
     AVEKITAAYN EGLVTDERLA YSVKKILHYK YKIGLNKYKP IDETNLMSDI NPSSNTALQY
     ELFENAITLL KNDNAILPIK ELDKKIAYVK LGDDTNAKFL STLKKYTDVT EVTSDNIDSL
     NVQLKNFDIV IVGFHKSDKA WKKHDFTETE LLWLQEIAKN NKVILDIFAK AYSLLPITTF
     DDIESVIVSY QNGDIPQEVS AELIFGAVDA KGKLPVSIND FFRVNDGLSS EKINRIGFTA
     PENVGMSSSK LATIETIAQK AIDEKMAPGM QILVARKGKV IYQKSFGYHT YENLTKVQNS
     DIYDVASITK MVSTLPNVMQ LYDQGKVTLD TKLGEMLPIF QGSDKQDITF KELLSHYARL
     QAWLPFYKET LDADNCPADR FYSLTYKDGY TKQVAENLFI NDNYKDVILK KIVDSKLSDK
     KEYKYSDFTF IILKEYLEKI TGKSLDILSA HNFYNMLGMS NTMYNPLRKF DMRIIPPTDN
     DTYFRHTTIQ GYVHDMEAAM EGGIAGHAGI FSNAMDVAKM MQMYLNKGNY GGIQYFSNAT
     FDVFNTCHFC TEGNRRGLGF DKPQLGKEGP TCGCVSMSSF GHTGFTGTMA WADPETEIIY
     VFLSNRTFPD SNASNKLSKE NIREDIQKII QEAIIK
//
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