ECMDB

Identification

Name:

Beta-hexosaminidase

Synonyms:

Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase

Gene Name:

nagZ

Enzyme Class:

3.2.1.52

Biological Properties

General Function:

Involved in beta-N-acetylhexosaminidase activity

Specific Function:

Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides

Cellular Location:

Cytoplasm

SMPDB Pathways:

1,6-anhydro-<i>N</i>-acetylmuramic acid recycling PW002064
Amino sugar and nucleotide sugar metabolism I PW000886
Amino sugar and nucleotide sugar metabolism II PW000887
Amino sugar and nucleotide sugar metabolism III PW000895

KEGG Pathways:

Amino sugar and nucleotide sugar metabolism ec00520
Glycosaminoglycan degradation ec00531
Glycosphingolipid biosynthesis - ganglio series ec00604
Glycosphingolipid biosynthesis - globo series ec00603
Metabolic pathways eco01100
Other glycan degradation ec00511

KEGG Reactions:

1.0

↔

2.0

1.0Chitobiose + 1.0Water ↔ 2.0N-Acetyl-D-glucosamine
ReactionCard

1.0

1.0Globoside

↔

1.0

1.0Globotriaosylceramide

1.0Water + 1.0Globoside ↔ 1.0N-Acetyl-b-D-galactosamine + 1.0Globotriaosylceramide
ReactionCard

1.0GM2

1.0

↔

1.0GM3

1.0

1.0GM2 + 1.0Water ↔ 1.0GM3 + 1.0N-Acetyl-b-D-galactosamine
ReactionCard

1.0G13033

1.0

↔

1.0G08421

1.0

1.0G13033 + 1.0Water ↔ 1.0G08421 + 1.0N-Acetyl-b-D-galactosamine
ReactionCard

1.0G06780

1.0

↔

1.0G08421

1.0

1.0G06780 + 1.0Water ↔ 1.0G08421 + 1.0N-Acetyl-b-D-galactosamine
ReactionCard

SMPDB Reactions:

1.0

1.0Chitobiose

1.0

→

2.0N-Acetyl-D-glucosamine

2.0

1.0Water + 1.0Chitobiose + 1.0Chitobiose → 2.0N-Acetyl-D-glucosamine + 2.0N-Acetylglucosamine
ReactionCard

1.0N-acetyl-β-D-glucosamine(anhydrous)-N-acetylmuramate

1.0

→

1.0

1.0anhydro-n-acetylmuramic acid

1.0N-acetyl-β-D-glucosamine(anhydrous)-N-acetylmuramate + 1.0Water → 1.0N-Acetylglucosamine + 1.0anhydro-n-acetylmuramic acid
ReactionCard

EcoCyc Reactions:

1.0an N-acetyl-β-D-hexosaminide

1.0

1.0an organic molecule

1.0an N-acetyl-β-D-hexosamine

1.0an N-acetyl-β-D-hexosaminide + 1.0Water ? 1.0an organic molecule + 1.0an N-acetyl-β-D-hexosamine
ReactionCard

1.0N-acetyl-β-D-glucosamine(anhydrous)-N-acetylmuramate

1.0

1.0N-acetyl-β-D-glucosamine(anhydrous)-N-acetylmuramate + 1.0Water ? 1.0N-Acetyl-D-glucosamine + 1.01,6-Anhydro-N-acetylmuramate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acid + 1.0Water → 1.0N-Acetyl-D-glucosamine + 1.01,6-Anhydro-N-acetylmuramate
ReactionCard

1.0

→

1.0

1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide + 1.0Water → 1.0N-Acetyl-D-glucosamine + 1.01,6-Anhydrous-N-Acetylmuramyl-tetrapeptide
ReactionCard

1.0

→

1.0

1.0N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide + 1.0Water → 1.0N-Acetyl-D-glucosamine + 1.01,6-Anhydrous-N-Acetylmuramyl-tripeptide
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB20519	1,6-Anhydro-N-acetylmuramate	MetaboCard
ECMDB21111	1,6-Anhydrous-N-Acetylmuramyl-tetrapeptide	MetaboCard
ECMDB21112	1,6-Anhydrous-N-Acetylmuramyl-tripeptide	MetaboCard
ECMDB03556	Chitobiose	MetaboCard
ECMDB00853	N-Acetyl-b-D-galactosamine	MetaboCard
ECMDB00215	N-Acetyl-D-glucosamine	MetaboCard
ECMDB21248	N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramic acid	MetaboCard
ECMDB21249	N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tetrapeptide	MetaboCard
ECMDB21250	N-Acetyl-D-glucosamine(anhydrous)N-Acetylmuramyl-tripeptide	MetaboCard
ECMDB21561	N-Acetylglucosamine	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
carbohydrate metabolic process
metabolic process
primary metabolic process

Gene Properties

Blattner:

b1107

Gene Orientation

Clockwise

Centisome Percentage:

25.07

Left Sequence End

1163318

Right Sequence End

1164343

Gene Sequence:

>1026 bp
ATGCCTTCAATTCGACTGGCTGATTTAGCGCAGCAGTTGGATGCAGAACTACACGGTGAT
GGCGATATCGTCATCACCGGCGTTGCGTCCATGCAATCTGCACAAACAGGTCACATTACG
TTCATGGTTAACCCAAAATACCGTGAGCATTTAGGCTTGTGCCAGGCGTCCGCGGTTGTC
ATGACCCAGGACGATCTTCCTTTCGCGAAAAGTGCCGCACTGGTAGTGAAGAATCCCTAC
CTGACTTACGCGCGCATGGCGCAAATTTTAGATACCACGCCGCAGCCCGCGCAGAACATT
GCACCCAGTGCGGTGATCGACGCGACGGCGAAGCTGGGTAACAACGTATCGATTGGCGCT
AACGCGGTGATTGAGTCCGGCGTTGAACTGGGCGATAACGTGATTATCGGTGCCGGTTGC
TTCGTAGGTAAAAACAGCAAAATCGGTGCAGGTTCGCGTCTCTGGGCGAACGTAACCATT
TACCATGAGATCCAGATCGGTCAGAATTGCCTGATCCAGTCCGGAACAGTGGTAGGCGCA
GACGGCTTTGGTTATGCCAACGATCGTGGTAACTGGGTGAAGATCCCACAGATTGGTCGC
GTAATTATTGGCGATCGCGTGGAGATCGGTGCCTGCACAACCATCGATCGCGGCGCGCTG
GATGACACTATTATTGGCAATGGCGTGATCATTGATAACCAGTGCCAGATTGCACATAAC
GTCGTGATTGGCGACAATACGGCGGTTGCCGGTGGCGTCATTATGGCGGGCAGCCTGAAA
ATTGGTCGTTACTGCATGATCGGCGGAGCCAGCGTAATCAACGGGCATATGGAAATATGC
GACAAAGTGACGGTTACGGGCATGGGTATGGTGATGCGTCCCATCACTGAACCAGGCGTC
TATTCCTCAGGCATTCCGCTGCAACCCAACAAAGTCTGGCGCAAAACCGCTGCACTGGTG
ATGAACATTGATGACATGAGCAAGCGTCTGAAATCGCTTGAGCGCAAGGTTAATCAACAA
GACTAA

Protein Properties

Pfam Domain Function:

Glyco_hydro_3 (PF00933 )

Protein Residues:

341

Protein Molecular Weight:

37594

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Beta-hexosaminidase
MGPVMLDVEGYELDAEEREILAHPLVGGLILFTRNYHDPAQLRELVRQIRAASRNRLVVA
VDQEGGRVQRFREGFTRLPAAQSFAALSGMEEGGKLAQEAGWLMASEMIAMDIDISFAPV
LDVGHISAAIGERSYHADPQKALAIASRFIDGMHEAGMKTTGKHFPGHGAVTADSHKETP
CDPRPQAEIRAKDMSVFSSLIRENKLDAIMPAHVIYSDVDPRPASGSPYWLKTVLRQELG
FDGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERV
TRLYHKGSFSRQELMDSARWKAISTRLNQLHERWQEEKAGH

References

External Links:

Resource	Link
Uniprot ID:	P75949
Uniprot Name:	NAGZ_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	4902920
Ecogene ID:	EG13433
Ecocyc:	EG13433
ColiBase:	b1107
Kegg Gene:	b1107
EchoBASE ID:	EB3207
CCDB:	NAGZ_ECOLI
BacMap:	16129070

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Cheng, Q., Li, H., Merdek, K., Park, J. T. (2000). "Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling." J Bacteriol 182:4836-4840. Pubmed: 10940025
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
Yem, D. W., Wu, H. C. (1976). "Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli." J Bacteriol 125:324-331. Pubmed: 1377

Beta-hexosaminidase (P75949)