ID A0A0G3LQH3_XANCT Unreviewed; 335 AA.
AC A0A0G3LQH3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:QEO25813.1};
GN ORFNames=F0H32_06125 {ECO:0000313|EMBL:QEO25813.1}, FD63_05880
GN {ECO:0000313|EMBL:AKK67042.1};
OS Xanthomonas translucens pv. undulosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=487909 {ECO:0000313|EMBL:QEO25813.1, ECO:0000313|Proteomes:UP000324457};
RN [1] {ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu4699 {ECO:0000313|Proteomes:UP000035194};
RA Peng Z., Potnis N., Jones J., Liu Z., White F.F., Liu S.;
RT "A complete genome of Xanthomonas translucens and the full TAL effector
RT gene content using long read sequencing.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK67042.1, ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu 4699 {ECO:0000313|EMBL:AKK67042.1}, and Xtu4699
RC {ECO:0000313|Proteomes:UP000035194};
RX PubMed=26729225; DOI=10.1186/s12864-015-2348-9;
RA Peng Z., Hu Y., Xie J., Potnis N., Akhunova A., Jones J., Liu Z.,
RA White F.F., Liu S.;
RT "Long read and single molecule DNA sequencing simplifies genome assembly
RT and TAL effector gene analysis of Xanthomonas translucens.";
RL BMC Genomics 17:21-21(2016).
RN [3] {ECO:0000313|EMBL:QEO25813.1, ECO:0000313|Proteomes:UP000324457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW16 {ECO:0000313|EMBL:QEO25813.1,
RC ECO:0000313|Proteomes:UP000324457};
RA Peng Z., Huguet-Tapia J.C., White F.;
RT "Xanthomonas translucens pv. undulosa LW16.";
RL Submitted (AUG-2019) 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}.
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DR EMBL; CP008714; AKK67042.1; -; Genomic_DNA.
DR EMBL; CP043540; QEO25813.1; -; Genomic_DNA.
DR RefSeq; WP_004426417.1; NZ_MADU01000022.1.
DR AlphaFoldDB; A0A0G3LQH3; -.
DR STRING; 487909.FD63_05880; -.
DR GeneID; 66887861; -.
DR KEGG; xtn:FD63_05880; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000035194; Chromosome.
DR Proteomes; UP000324457; Chromosome.
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}.
FT DOMAIN 4..292
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 335 AA; 35589 MW; 86CBBCE50079301A CRC64;
MLAIGVAGTE LTAQERDWLQ HDAVAGVVLF KRNFASRAQL VELTAAIRAA APRPQLICVD
QEGGRVQRFR EGYSALPPLH GFGALYARDR DAALALAEQH AWLMASEVRA SGVDLSFAPV
VDLARGNRAI GDRAFSDDPQ VVAAFTAAYV RGMHSVGMAA TLKHFPGHGT VLEDTHVDNA
EDPRPLEVLR QEDLLPFAAG IAAGADAVMM AHVVYPQVAP EPAGYSSRWI QQILRQELGF
RGVVFSDDIG MAASFAAGGV AARVSAHLDA GCDVVLVCHP ELVEDALQAV RERPLNTAAL
LGLIGRGALG WDGLLADARY GHTQSHLLAT LGKTA
//
