NAGZ_SHEON
ID NAGZ_SHEON Reviewed; 342 AA.
AC Q8EEW2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SO_2250;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00364};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_00364}.
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; AE014299; AAN55290.1; -; Genomic_DNA.
DR RefSeq; NP_717846.1; NC_004347.2.
DR RefSeq; WP_011072263.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EEW2; -.
DR SMR; Q8EEW2; -.
DR STRING; 211586.SO_2250; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PaxDb; Q8EEW2; -.
DR KEGG; son:SO_2250; -.
DR PATRIC; fig|211586.12.peg.2166; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_0_0_6; -.
DR OMA; WQMAAEM; -.
DR OrthoDB; 949956at2; -.
DR PhylomeDB; Q8EEW2; -.
DR BioCyc; SONE211586:G1GMP-2055-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000008186; 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; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Glycosidase; Hydrolase; Peptidoglycan synthesis;
KW Reference proteome.
FT CHAIN 1..342
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000210798"
FT ACT_SITE 177
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 249
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 164..165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 175
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
SQ SEQUENCE 342 AA; 37193 MW; AB603E9104D16065 CRC64;
MSYLMLDLLS LDVSEAEAEM LRHPQVGGLI LFSRNFTSRE QLIALVQQIR QIRPEILIAV
DHEGGRVQRF REGFTLIPAM GDILPAAKGD MALAKRWACE LGFLMAIELL ACDIDLSFAP
VLDLNGISQV IGKRSFSANP DEVIALARSF IEGMAQAGMG AVGKHFPGHG SVAADSHIAQ
PIDEREGEVI FNQDILPFKE LIFNGKLSGI MPAHVIYPKV DPNPAGFSSY WLKQILRKEL
GFNGVIFSDD LGMKGASFAG DYVGRAKAAL DAGCDMILVC NDNPGVMTLL NGFVWPEAAP
QHPASLLKPN MAQTALALEN SARWENAKQL AEQIQLAQQA KV
