Endo-beta-N-acetylglucosaminidase - Arthrobacter protophormiae

Preferred order of sections

Names and origin

Protein names	Submitted name: Endo-beta-N-acetylglucosaminidase EMBL AAD10851.1 EC=3.2.1.96 EMBL AAD10851.1
Organism	Arthrobacter protophormiae EMBL AAD10851.1
Taxonomic identifier	37930 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	645 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 3FHA Metal-binding PDB 3FHA
Molecular function	Glycosidase EMBL AAD10851.1 Hydrolase
Technical term	3D-structure PDB 3FHQ PDB 3FHA PDB 2VTF
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

333

1

Calcium PDB 3FHA

Metal binding

390

1

Calcium; via carbonyl oxygen PDB 3FHA

Metal binding

401

1

Calcium PDB 3FHA

Binding site

119

1

Mannose; via carbonyl oxygen PDB 3FHQ

Binding site

155

1

Beta-D-mannose PDB 3FHQ

Binding site

296

1

Beta-D-mannose PDB 3FHQ

Binding site

323

1

Beta-D-mannose PDB 3FHQ

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZB22 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F4AF0B1E2A3AF2A4
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FASTA

645

72,091

        10         20         30         40         50         60 
MRKAFLVGLV CTACVLLHDD PVAASTYNGP LSSHWFPEEL AQWEPDSDPD APFNRSHVPL 

        70         80         90        100        110        120 
EPGRVANRVN ANADKDAHLV SLSALNRHTS GVPSQGAPVF YENTFSYWHY TDLMVYWAGS 

       130        140        150        160        170        180 
AGEGIIVPPS ADVIDASHRN GVPILGNVFF PPTVYGGQLE WLEQMLEQEE DGSFPLADKL 

       190        200        210        220        230        240 
LEVADYYGFD GWFINQETEG ADEGTAEAMQ AFLVYLQEQK PEGMHIMWYD SMIDTGAIAW 

       250        260        270        280        290        300 
QNHLTDRNKM YLQNGSTRVA DSMFLNFWWR DQRQSNELAQ ALGRSPYDLY AGVDVEARGT 

       310        320        330        340        350        360 
STPVQWEGLF PEGEKAHTSL GLYRPDWAFQ SSETMEAFYE KELQFWVGST GNPAETDGQS 

       370        380        390        400        410        420 
NWPGMAHWFP AKSTATSVPF VTHFNTGSGA QFSAEGKTVS EQEWNNRSLQ DVLPTWRWIQ 

       430        440        450        460        470        480 
HGGDLEATFS WEEAFEGGSS LQWHGSLAEG EHAQIELYQT ELPISEGTSL TWTFKSEHGN 

       490        500        510        520        530        540 
DLNVGFRLDG EEDFRYVEGE QRESINGWTQ WTLPLDAFAG QTITGLAFAA EGNETGLAEF 

       550        560        570        580        590        600 
YIGQLAVGAD SEKPAAPNVN VRQYDPDPSG IQLVWEKQSN VHHYRVYKET KHGKELIGTS 

       610        620        630        640 
AGDRIYLEGL VEESKQNDVR LHIEALSETF VPSDARMIDI KSGSF

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References

[1]	"Arthrobacter protophormiae Endo-beta-N-acetylglucosaminidase gene." Takegawa K., Yamabe K., Fujita K., Tabuchi M., Mita M., Izu H., Watanabe A., Asada Y., Sano M., Kondo A., Kato I., Iwahara S. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: AKU 0647 EMBL AAD10851.1.
[2]	"The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity." Ling Z., Suits M.D., Bingham R.J., Bruce N.C., Davies G.J., Fairbanks A.J., Moir J.W., Taylor E.J. J. Mol. Biol. 389:1-9(2009) [PubMed: 19327363] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 25-645.
[3]	"Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A." Yin J., Li L., Shaw N., Li Y., Song J.K., Zhang W., Xia C., Zhang R., Joachimiak A., Zhang H.C., Wang L.X., Liu Z.J., Wang P. PLoS ONE 4:e4658-e4658(2009) [PubMed: 19252736] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-645 IN COMPLEX WITH BETA-D-MANNOSE; CALCIUM AND MANNOSE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U59168 Genomic DNA. Translation: AAD10851.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VTF	X-ray	1.79	A/B	25-645	[»]
3FHA	X-ray	2.00	A/B/C/D	25-645	[»]
3FHQ	X-ray	2.45	A/B/D/F	25-645	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH85. Glycoside Hydrolase Family 85.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005201. Glyco_hydro_85.
[Graphical view]

Pfam

PF03644. Glyco_hydro_85. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9ZB22_9MICC

Accession

Primary (citable) accession number: Q9ZB22

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	July 27, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)