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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.UniRule annotation

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661SubstrateUniRule annotation
Binding sitei74 – 741SubstrateUniRule annotation
Binding sitei140 – 1401SubstrateUniRule annotation
Sitei181 – 1811Important for catalytic activityUniRule annotation
Active sitei183 – 1831Proton donor/acceptorUniRule annotation
Active sitei254 – 2541NucleophileUniRule annotation

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB-KW
  4. cell wall organization Source: UniProtKB-KW
  5. peptidoglycan biosynthetic process Source: UniProtKB-KW
  6. peptidoglycan turnover Source: UniProtKB-HAMAP
  7. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciCVIO243365:GHUD-2128-MONOMER.
UniPathwayiUPA00544.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidaseUniRule annotation (EC:3.2.1.52UniRule annotation)
Alternative name(s):
Beta-N-acetylhexosaminidaseUniRule annotation
N-acetyl-beta-glucosaminidaseUniRule annotation
Gene namesi
Name:nagZUniRule annotation
Ordered Locus Names:CV_2073
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
ProteomesiUP000001424 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Beta-hexosaminidasePRO_0000210784Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243365.CV_2073.

Structurei

3D structure databases

ProteinModelPortaliQ7NWB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 1712Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
KOiK01207.
OMAiHILALYE.
OrthoDBiEOG6BCT06.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7NWB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLPRGPVMV DIAGFALTEA ERARLSHPLV GGVILFRRNF HNIEQLRALT
60 70 80 90 100
AEIRALRTPH LLIAVDHEGG RVQRFLDGFT RLPPMRVLGE AWDADRDQAL
110 120 130 140 150
KLAETVGYVL AAELSACGID LSFTPVLDLD WERCAVIGNR AFHRDPEAVS
160 170 180 190 200
ALAEALQQGL GRGGMMSCGK HYPGHGYVEG DSHHLMPQDD RTLAQIEQDD
210 220 230 240 250
LVPFARLADA GMGAVMPAHV LYPAVDSQPA GFSKVWLTDI LRGRIGFDGV
260 270 280 290 300
IFSDALDMAG AAGAGTYVQR ADAALAAGCD MVLVCNQPEE ADAMLAALAP
310 320 330 340 350
PPQPQLAERL ERMAGKSRAE DWQRLIATPD FAAAQAAVRQ LAMPKDALAG

PQVGEAH
Length:357
Mass (Da):38,401
Last modified:December 15, 2003 - v1
Checksum:i21061E9289B8BE92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ59745.2.
RefSeqiNP_901743.1. NC_005085.1.
WP_011135621.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ59745; AAQ59745; CV_2073.
GeneIDi2547871.
KEGGicvi:CV_2073.
PATRICi21438936. VBIChrVio67196_2024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ59745.2.
RefSeqiNP_901743.1. NC_005085.1.
WP_011135621.1. NC_005085.1.

3D structure databases

ProteinModelPortaliQ7NWB7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_2073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ59745; AAQ59745; CV_2073.
GeneIDi2547871.
KEGGicvi:CV_2073.
PATRICi21438936. VBIChrVio67196_2024.

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
KOiK01207.
OMAiHILALYE.
OrthoDBiEOG6BCT06.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciCVIO243365:GHUD-2128-MONOMER.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
    Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
    , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Entry informationi

Entry nameiNAGZ_CHRVO
AccessioniPrimary (citable) accession number: Q7NWB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: April 1, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.