ID A0A0A0F291_9GAMM Unreviewed; 331 AA.
AC A0A0A0F291;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=N800_14520 {ECO:0000313|EMBL:KGM55517.1};
OS Lysobacter daejeonensis GH1-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM55517.1, ECO:0000313|Proteomes:UP000029998};
RN [1] {ECO:0000313|EMBL:KGM55517.1, ECO:0000313|Proteomes:UP000029998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH1-9 {ECO:0000313|EMBL:KGM55517.1,
RC ECO:0000313|Proteomes:UP000029998};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) 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:KGM55517.1}.
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DR EMBL; AVPU01000005; KGM55517.1; -; Genomic_DNA.
DR RefSeq; WP_036135404.1; NZ_AVPU01000005.1.
DR AlphaFoldDB; A0A0A0F291; -.
DR STRING; 1385517.N800_14520; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9786661at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000029998; 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|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW 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:UP000029998}.
FT DOMAIN 3..296
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 331 AA; 35774 MW; A83398EFF0EF5832 CRC64;
MLVIGVAGTE LTAQERDWLQ HDACAGVILF SRNFASKAQV AELSQAIREA APRPQLVCVD
QEGGRVQRFR EGYSALPPLE HFGRLYAQDK AAALAMAEEH AWLMACEVRA TGVDLSFAPV
VDLGRGNRAI GNRAFSEDPA VVADFTRAYV RGMHSAGMAA TLKHFPGHGS VLEDTHFDDA
IDPRPLDEIR ALDLVPFVAG IEAKADAVMM AHVVYPAVAP EPAGYSKVWI EDILRKEMGF
RGVVFSDDIG MAAAFSAGGI KQRVDLHLDA GCDVVLVCHP ELVEESLDAI KDRKLNTMAL
TGLIGRGPMG WDGLLADARY AQARTRQEGI A
//
