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Database: UniProt
Entry: A0A014NP94_9BURK
LinkDB: A0A014NP94_9BURK
Original site: A0A014NP94_9BURK 
ID   A0A014NP94_9BURK        Unreviewed;       364 AA.
AC   A0A014NP94;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=AX13_10615 {ECO:0000313|EMBL:EXU81248.1};
OS   Comamonas aquatica DA1877.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU81248.1, ECO:0000313|Proteomes:UP000020766};
RN   [1] {ECO:0000313|EMBL:EXU81248.1, ECO:0000313|Proteomes:UP000020766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA1877 {ECO:0000313|EMBL:EXU81248.1,
RC   ECO:0000313|Proteomes:UP000020766};
RA   Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA   Caudy A.A., Walhout A.J.;
RT   "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT   Gene Expression and Life History Traits.";
RL   Submitted (JAN-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:EXU81248.1}.
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DR   EMBL; JBOK01000003; EXU81248.1; -; Genomic_DNA.
DR   RefSeq; WP_043379593.1; NZ_JBOK01000003.1.
DR   AlphaFoldDB; A0A014NP94; -.
DR   STRING; 225991.MA05_15045; -.
DR   PATRIC; fig|1457173.3.peg.649; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000020766; 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; 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.
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:UP000020766}.
FT   DOMAIN          14..314
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   BINDING         181..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT   SITE            192
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ   SEQUENCE   364 AA;  39674 MW;  14E71A51BFE26A79 CRC64;
     MTALHAPLII DIAGKALTDT DRDRLAHPLV GGIILFTRNW EDRAQLVQLC ADIKAVKPDL
     LICVDHEGGR VQRFKTDGFT HLPPMRAFGE MWMDDGKGKK RHKGHGAMRA MNAATAAGYV
     LGSELRACGV DFSFTPVLDL DHGASGVIGD RSFHRDPRVV AALAKSLMHG LLQAGMGNCG
     KHFPGHGHVT LDSHVDMPVD KRKLKKILAD DAAPYPWLSS VLTAVMPAHV IYPKVDALPA
     GFSKVWLQDV LRGELRYDGA IFSDDLSMEA ARRIDGQVIS YTEAALRALA AGCDMVLLCN
     QSLGLGAHVD ELLDGMDDAL RTGRWVPDAD SESRRVALLP ETVPQPWDEL MLQPAYRDAL
     GLLK
//
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