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Database: UniProt
Entry: A0A0A2WGL7_9GAMM
LinkDB: A0A0A2WGL7_9GAMM
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ID   A0A0A2WGL7_9GAMM        Unreviewed;       332 AA.
AC   A0A0A2WGL7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE            EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
GN   Name=nagZ {ECO:0000256|HAMAP-Rule:MF_00364};
GN   ORFNames=LF41_167 {ECO:0000313|EMBL:KGQ18928.1};
OS   Lysobacter dokdonensis DS-58.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18928.1, ECO:0000313|Proteomes:UP000030518};
RN   [1] {ECO:0000313|EMBL:KGQ18928.1, ECO:0000313|Proteomes:UP000030518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18928.1,
RC   ECO:0000313|Proteomes:UP000030518};
RA   Kim J.F., Kwak M.-J.;
RT   "Genome sequences of Lysobacter dokdonensis DS-58.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC       terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC       linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC       acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
CC       {ECO:0000256|HAMAP-Rule:MF_00364}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00364};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_00364}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00364}.
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:KGQ18928.1}.
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DR   EMBL; JRKJ01000011; KGQ18928.1; -; Genomic_DNA.
DR   RefSeq; WP_036169010.1; NZ_JRKJ01000011.1.
DR   AlphaFoldDB; A0A0A2WGL7; -.
DR   STRING; 1300345.LF41_167; -.
DR   PATRIC; fig|1300345.3.peg.1845; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9786661at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000030518; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   HAMAP; MF_00364; NagZ; 1.
DR   InterPro; IPR022956; Beta_hexosaminidase_bac.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
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; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00364};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00364};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00364};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00364};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00364};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00364};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00364};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00364}; Reference proteome {ECO:0000313|Proteomes:UP000030518}.
FT   DOMAIN          5..285
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   ACT_SITE        176
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         163..164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   SITE            174
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   332 AA;  35633 MW;  38E5247F244B9606 CRC64;
     MLVIGIAGTE LTAQERDWLQ HDACAGVILF TRNFSSRVQV AELSQAIREA APRPQLICVD
     QEGGRVQRFR DGYSALPSLE QFGKLYGSLP DRAIELAKEH AWVMASEVRA SGVDLSFAPV
     VDLGRGNRAI GDRAFSADPQ IVAEFTRAYV EGMHAADMAA TLKHFPGHGS VLEDTHFDDA
     IDKRTLDEIR ALDLVPFVAG IDAGADAVMM AHVVYPQVAP EPAGYSPLWI EQILRKEMGF
     KGVVFSDDIG MAAAFSAGGV KSRIDAHLDA GCDVVLVCHP DLVPDSLAAV EGRKLNTMAL
     AGLIGRGPLA WEGLLADARY TDAHARFGGD LA
//
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