Reviewed, UniProtKB/Swiss-Prot A4Q8F7 (GH109_FLAME)

Names and origin

Protein names

Recommended name:
    Alpha-N-acetylgalactosaminidase
    EC=3.2.1.49
Alternative name(s):
    Glycosyl hydrolase family 109 protein

Gene names

Name:

nagA

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Glycosidase that has specific alpha-N-acetylgalactosaminidase activity. Ref.1
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides. Ref.1
Cofactor	Binds 1 NAD+ per subunit. The NAD cannot dissociate. Ref.1
Biotechnological use	Specifically cleaves the blood group A antigen at neutral pH with low consumption of recombinant enzyme. It is therefore a good candidate to participate to the development of universal red blood cells by removing blood group A antigen. Ref.1
Sequence similarities	Belongs to the gfo/idh/mocA family. Glycosyl hydrolase 109 subfamily.
biophysicochemical properties	Kinetic parameters: KM=25.1 mM for Galalpha-pNP KM=3.6 mM for Galbeta-pNP KM=0.077 mM for GalNAcalpha-pNP KM=0.23 mM for GalNAcbeta-pNP pH dependence: Optimum pH is 6.8.

Ontologies

Keywords
Ligand	NAD
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-N-acetylgalactosaminidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Alpha-N-acetylgalactosaminidase		PRO_0000348545
Regions
	Nucleotide binding	30 – 31	2	NAD
	Nucleotide binding	101 – 104	4	NAD
	Nucleotide binding	121 – 122	2	NAD
	Nucleotide binding	208 – 212	5	NAD
	Region	225 – 228	4	Substrate binding
Sites
	Binding site	52	1	NAD
	Binding site	80	1	NAD; via carbonyl oxygen
	Binding site	107	1	NAD
	Binding site	150	1	NAD
	Binding site	179	1	Substrate
	Binding site	213	1	Substrate
	Binding site	225	1	NAD
	Binding site	307	1	Substrate

Sequences

	Sequence		Length	Mass (Da)
	A4Q8F7-1 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 31457EDBC89518FB	FASTA	444	50,211
	10 20 30 40 50 60 MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF ADPDPYMVGR 70 80 90 100 110 120 AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP WEWHHEHGVA AMKAGKIVGM 130 140 150 160 170 180 EVSGAITLEE CWDYVKVSEQ TGVPLMALEN VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ 190 200 210 220 230 240 HDLRPVLFNS GINGKNGDGV EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN 250 260 270 280 290 300 RGNRLLRLSS FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD 310 320 330 340 350 360 TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK WIKEYDHPMW 370 380 390 400 410 420 KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL ATWYSITPLS EKSIAENGAV 430 440 QEIPDFTNGK WKNAKNTFAI NDDY

References

[1]

"Bacterial glycosidases for the production of universal red blood cells." Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K., Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S., Bourne Y., Olsson M.L., Henrissat B., Clausen H. Nat. Biotechnol. 25:454-464(2007) [PubMed: 17401360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). Strain: ATCC 33958.

Web resources

Protein Spotlight

The juice of life - Issue 98 of October 2008

Cross-references

Sequence databases

EMBLGenBankDDBJ

AM039444 Genomic DNA. Translation: CAJ01376.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IXA	X-ray	2.30	A	1-444	[»]
2IXB	X-ray	2.40	A	1-444	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GH109_FLAME

Accession

Primary (citable) accession number: A4Q8F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	May 15, 2007
Last modified:	June 16, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)