NAGZ_NEIG1
ID NAGZ_NEIG1 Reviewed; 361 AA.
AC Q5FA94;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=NGO0135;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) 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: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; AE004969; AAW88893.1; -; Genomic_DNA.
DR RefSeq; WP_003704881.1; NC_002946.2.
DR RefSeq; YP_207305.1; NC_002946.2.
DR PDB; 6JTI; X-ray; 2.20 A; A/B/C/D/E/F=1-361.
DR PDB; 6JTJ; X-ray; 2.18 A; A/B/C/D/E/F=1-361.
DR PDB; 6JTK; X-ray; 2.20 A; A/B/C/D/E/F=1-361.
DR PDB; 6JTL; X-ray; 2.40 A; A/B=1-361.
DR PDBsum; 6JTI; -.
DR PDBsum; 6JTJ; -.
DR PDBsum; 6JTK; -.
DR PDBsum; 6JTL; -.
DR AlphaFoldDB; Q5FA94; -.
DR SMR; Q5FA94; -.
DR STRING; 242231.NGO_0135; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblBacteria; AAW88893; AAW88893; NGO_0135.
DR KEGG; ngo:NGO_0135; -.
DR PATRIC; fig|242231.10.peg.173; -.
DR HOGENOM; CLU_008392_0_0_4; -.
DR OMA; WQMAAEM; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000535; 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; -; 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; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycosidase; Hydrolase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..361
FT /note="Beta-hexosaminidase"
FT /id="PRO_0000234917"
FT ACT_SITE 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT BINDING 174..175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT SITE 185
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00364"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:6JTJ"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6JTJ"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:6JTJ"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6JTJ"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:6JTJ"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:6JTJ"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:6JTJ"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:6JTJ"
SQ SEQUENCE 361 AA; 39033 MW; AABBC553B4BEA82C CRC64;
MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAIGGIILFR RNFQNIEQLK TLTAEIKALR
TPELIIAVDH EGGRVQRFIE GFTRLPAMNV LGQIWDKDGA SAAETAAGQV GRVLATELSA
CGIDLSFTPV LDLDWGNCAV IGNRSFHRNP EAVARLALAL QKGLAKGGMK SCGKHFPGHG
FVEGDSHLVL PEDGRSLDEL EAADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW
LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRD
GFTIPDNQDL AGRWQYMENS LGHEAVQAVM QTMGFQAAQA FVAGLASPQD TAGGVKVGEA
F
