NAGZ_VIBCH
ID NAGZ_VIBCH Reviewed; 330 AA.
AC Q9KU37;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364};
GN Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364}; OrderedLocusNames=VC_0692;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24009110; DOI=10.1002/cbic.201300395;
RA Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E.,
RA Gloster T.M., Vocadlo D.J., Mark B.L.;
RT "The development of selective inhibitors of NagZ: increased susceptibility
RT of Gram-negative bacteria to beta-lactams.";
RL ChemBioChem 14:1973-1981(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP N-ACETYL-D-GLUCOSAMINE.
RA Gorman J., Shapiro L.;
RT "Structure of beta-hexosaminidase from Vibrio cholerae in complex with N-
RT acetyl-D-glucosamine.";
RL Submitted (DEC-2004) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17439950; DOI=10.1074/jbc.m700084200;
RA Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J.;
RT "Small molecule inhibitors of a glycoside hydrolase attenuate inducible
RT AmpC-mediated beta-lactam resistance.";
RL J. Biol. Chem. 282:21382-21391(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=19499593; DOI=10.1002/pro.137;
RA Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J.,
RA Mark B.L.;
RT "Insight into a strategy for attenuating AmpC-mediated beta-lactam
RT resistance: structural basis for selective inhibition of the glycoside
RT hydrolase NagZ.";
RL Protein Sci. 18:1541-1551(2009).
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 Plays a role in beta-lactam antibiotic resistance via its role in
CC generating anhydro-N-acetylmuramic acid-linked peptides; these peptides
CC function as signaling molecules that induce high-level expression of
CC the beta-lactamase AmpC. {ECO:0000255|HAMAP-Rule:MF_00364,
CC ECO:0000269|PubMed:17439950, ECO:0000269|PubMed:19499593,
CC ECO:0000269|PubMed:24009110}.
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:0000255|HAMAP-Rule:MF_00364,
CC ECO:0000269|PubMed:17439950, ECO:0000269|PubMed:19499593,
CC ECO:0000269|PubMed:24009110};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
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DR EMBL; AE003852; AAF93857.1; -; Genomic_DNA.
DR PIR; A82292; A82292.
DR RefSeq; NP_230341.1; NC_002505.1.
DR RefSeq; WP_000529115.1; NZ_LT906614.1.
DR PDB; 1TR9; X-ray; 1.80 A; A=2-330.
DR PDB; 1Y65; X-ray; 1.85 A; A=2-330.
DR PDB; 2OXN; X-ray; 1.70 A; A=1-330.
DR PDB; 3GS6; X-ray; 2.30 A; A=1-330.
DR PDB; 3GSM; X-ray; 2.40 A; A=1-330.
DR PDBsum; 1TR9; -.
DR PDBsum; 1Y65; -.
DR PDBsum; 2OXN; -.
DR PDBsum; 3GS6; -.
DR PDBsum; 3GSM; -.
DR AlphaFoldDB; Q9KU37; -.
DR SMR; Q9KU37; -.
DR STRING; 243277.VC_0692; -.
DR ChEMBL; CHEMBL1075035; -.
DR DrugBank; DB07432; [[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamate.
DR DrugBank; DB08704; [[(3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-(pentanoylamino)oxan-2-ylidene]amino] N-phenylcarbamate.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR DNASU; 2615481; -.
DR EnsemblBacteria; AAF93857; AAF93857; VC_0692.
DR GeneID; 57739406; -.
DR KEGG; vch:VC_0692; -.
DR PATRIC; fig|243277.26.peg.663; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_0_0_6; -.
DR OMA; WQMAAEM; -.
DR BioCyc; VCHO:VC0692-MON; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; Q9KU37; -.
DR Proteomes; UP000000584; Chromosome 1.
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; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.300; -; 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 Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycosidase; Hydrolase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..330
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000210800"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 242
FT /note="Nucleophile"
FT BINDING 62
FT /ligand="substrate"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 130
FT /ligand="substrate"
FT BINDING 160..161
FT /ligand="substrate"
FT SITE 171
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:2OXN"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2OXN"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2OXN"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:2OXN"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:2OXN"
FT HELIX 312..328
FT /evidence="ECO:0007829|PDB:2OXN"
SQ SEQUENCE 330 AA; 36466 MW; A737BD82C149D3A2 CRC64;
MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR QAAKRPILIG
VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL MAAELIAHDV DLSFAPVLDM
GFACKAIGNR AFGEDVQTVL KHSSAFLRGM KAVGMATTGK HFPGHGAVIA DSHLETPYDE
RETIAQDMAI FRAQIEAGVL DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF
SDDLSMEGAA VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK
QQFSYSELKR LERWQQASAN MQRLIEQFSE
