Q619W7 (HEXA_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase A
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase

Gene names

Name:	hex-1
ORF Names:	CBG14058

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. Degrades chitotriose By similarity. UniProtKB Q22492
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. UniProtKB P06865
Subcellular location	Lysosome By similarity UniProtKB P06865.
Sequence similarities	Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-N-acetylhexosaminidase activity Inferred from sequence or structural similarity. Source: UniProtKB cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential
	Chain	16 – 552	537	Beta-hexosaminidase A		PRO_0000312664
Sites
	Active site	322	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	348	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Glycosylation	457	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q619W7 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: F51F5E37E49720A0	FASTA	552	63,880
	10 20 30 40 50 60 MRLIVLSLLF TSTLAWFYGR DEPDRWSVGG VWPLPQKIIY GSKNRTLTYD KIGIDLGDKK 70 80 90 100 110 120 DCDVLLAMAD NYMNKWLFPY PVEMKTGGTE DFIITVTVKE ECPGGPPVHG ASEEYLLRVS 130 140 150 160 170 180 VSEAVINAQT VWGALRAMET LSHLVFYDQK SQEYQIRTAE IFDKPRFPVR GIMIDSSRHF 190 200 210 220 230 240 LSLNVIKRQL EIMSMNKLNV LHWHLVDSES FPYTSQKFPE LHGVGAYSPR HVYSREDISE 250 260 270 280 290 300 VIAFARLRGI RVIPEFDLPG HTSSWKGRKG FLTECFDEKG EETFLPNLVD PMNDANFDFL 310 320 330 340 350 360 AEFLEEVTET FPDQFLHLGG DEVSDYIVEC WVRNKKIRKF MDEKGFGNNT VLLENYFFEK 370 380 390 400 410 420 LFSIVEKLKL KRKPIFWQEV FDNNIPDPNS IIHIWKGNTH EEIYEQVKNI TSKNFPVIVS 430 440 450 460 470 480 ACWYLNYIKY GADWRDEIRG TAPSNSRYYY CDPTSFNGTD TQKNLVLGGI AAIWGELVDN 490 500 510 520 530 540 TNIEARLWPR ASAAAERLWS PAEKTQKAEN AWPRMHELRC RLVSRGYRIQ PNNNPDYCPF 550 EFDEPPATKS EL

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000521 Genomic DNA. Translation: CAP32722.2.
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
ModBase	Search...
Protein-protein interaction databases
STRING	Q619W7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
WormBase	CBG14058; CBP29009; WBGene00034691.
Phylogenomic databases
HOGENOM	HBG591688.
Family and domain databases
InterPro	IPR015882. Acetylhexosaminidase_sua/b. IPR001540. Glyco_hydro_20. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HEXA_CAEBR

Accession

Primary (citable) accession number: Q619W7
Secondary accession number(s): A8XJ97

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	September 22, 2009
Last modified:	December 14, 2011
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project