ID A0A0W8JJY4_9VIBR Unreviewed; 328 AA.
AC A0A0W8JJY4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=VRK_06100 {ECO:0000313|EMBL:KUJ00479.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUJ00479.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUJ00479.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUJ00479.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) 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:KUJ00479.1}.
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DR EMBL; LQIY01000003; KUJ00479.1; -; Genomic_DNA.
DR RefSeq; WP_059120025.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JJY4; -.
DR STRING; 1761910.VRK_06100; -.
DR PATRIC; fig|1761910.3.peg.610; -.
DR OrthoDB; 9786661at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000054473; 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}.
FT DOMAIN 12..287
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 160..161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT SITE 171
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ SEQUENCE 328 AA; 36187 MW; 11030C38C5D05AC0 CRC64;
MGPLWLDVEG CELSAEEKEM LAHPTVGGVI LFARNYFDSR QLQALTQSIR QYARQPILLG
VDQEGGRVQR FQDGFTRLPA AASYARFPES ERLAQLGGWL MASELIAHDI DLSFAPVLDT
GFSCRAIGNR AFGDDDETVI SMSRAYIQGM KSAGMATTGK HFPGHGGVVE DSHKETPYDH
REDIFDTDMQ VFRQHIQANL LDAIMPAHVI YSHYDQQPAS GSAFWLKQIL RHKLGFNGII
FSDDLAMEGA SIMGDAVARS HQALAAGCDM LLLCNDRDAS VRVLDHLPIM AVSGAESLQK
QRSFNPAELK ATPQWKQAVA ALRPLTEE
//
