Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A4Q8F7

- GH109_ELIME

UniProt

A4Q8F7 - GH109_ELIME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-N-acetylgalactosaminidase

Gene

nagA

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Glycosidase that has specific alpha-N-acetylgalactosaminidase activity.1 Publication

Catalytic activityi

Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.1 Publication

Cofactori

NAD(+)1 PublicationNote: Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.1 Publication

Kineticsi

  1. KM=25.1 mM for Galalpha-pNP1 Publication
  2. KM=3.6 mM for Galbeta-pNP1 Publication
  3. KM=0.077 mM for GalNAcalpha-pNP1 Publication
  4. KM=0.23 mM for GalNAcbeta-pNP1 Publication

pH dependencei

Optimum pH is 6.8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521NAD
Binding sitei80 – 801NAD; via carbonyl oxygen
Binding sitei107 – 1071NAD
Binding sitei150 – 1501NAD
Binding sitei179 – 1791Substrate
Binding sitei213 – 2131Substrate
Binding sitei225 – 2251NAD
Binding sitei307 – 3071Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 312NAD
Nucleotide bindingi101 – 1044NAD
Nucleotide bindingi121 – 1222NAD
Nucleotide bindingi208 – 2125NAD

GO - Molecular functioni

  1. alpha-N-acetylgalactosaminidase activity Source: UniProtKB-EC
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

NAD

Protein family/group databases

CAZyiGH109. Glycoside Hydrolase Family 109.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
Alternative name(s):
Glycosyl hydrolase family 109 protein
Gene namesi
Name:nagA
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Pathology & Biotechi

Biotechnological usei

Specifically cleaves the blood group A antigen at neutral pH with low consumption of recombinant enzyme. It is therefore a good candidate to participate in the development of universal red blood cells by removing blood group A antigen.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Alpha-N-acetylgalactosaminidasePRO_0000348545Add
BLAST

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 266Combined sources
Helixi30 – 4011Combined sources
Beta strandi45 – 517Combined sources
Helixi55 – 6713Combined sources
Beta strandi74 – 763Combined sources
Turni80 – 823Combined sources
Helixi83 – 864Combined sources
Beta strandi94 – 974Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 11310Combined sources
Beta strandi117 – 1204Combined sources
Helixi128 – 14114Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 1534Combined sources
Helixi155 – 16511Combined sources
Turni166 – 1694Combined sources
Beta strandi171 – 1777Combined sources
Helixi184 – 1874Combined sources
Helixi208 – 2114Combined sources
Helixi213 – 2197Combined sources
Helixi227 – 23711Combined sources
Turni240 – 2423Combined sources
Beta strandi245 – 2528Combined sources
Helixi257 – 26610Combined sources
Helixi271 – 2744Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi294 – 3007Combined sources
Beta strandi312 – 3176Combined sources
Beta strandi319 – 3224Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi330 – 3345Combined sources
Turni336 – 3416Combined sources
Beta strandi346 – 3483Combined sources
Helixi349 – 3546Combined sources
Helixi358 – 36710Combined sources
Helixi375 – 38915Combined sources
Helixi397 – 41519Combined sources
Turni416 – 4183Combined sources
Turni426 – 4338Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IXAX-ray2.30A1-444[»]
2IXBX-ray2.40A1-444[»]
ProteinModelPortaliA4Q8F7.
SMRiA4Q8F7. Positions 19-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA4Q8F7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 2284Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4Q8F7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF
60 70 80 90 100
ADPDPYMVGR AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP
110 120 130 140 150
WEWHHEHGVA AMKAGKIVGM EVSGAITLEE CWDYVKVSEQ TGVPLMALEN
160 170 180 190 200
VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ HDLRPVLFNS GINGKNGDGV
210 220 230 240 250
EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN RGNRLLRLSS
260 270 280 290 300
FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD
310 320 330 340 350
TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK
360 370 380 390 400
WIKEYDHPMW KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL
410 420 430 440
ATWYSITPLS EKSIAENGAV QEIPDFTNGK WKNAKNTFAI NDDY
Length:444
Mass (Da):50,211
Last modified:May 15, 2007 - v1
Checksum:i31457EDBC89518FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM039444 Genomic DNA. Translation: CAJ01376.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

The juice of life - Issue 98 of October 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM039444 Genomic DNA. Translation: CAJ01376.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IXA X-ray 2.30 A 1-444 [» ]
2IXB X-ray 2.40 A 1-444 [» ]
ProteinModelPortali A4Q8F7.
SMRi A4Q8F7. Positions 19-444.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH109. Glycoside Hydrolase Family 109.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei A4Q8F7.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view ]
Pfami PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    Strain: ATCC 33958.

Entry informationi

Entry nameiGH109_ELIME
AccessioniPrimary (citable) accession number: A4Q8F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 15, 2007
Last modified: November 26, 2014
This is version 39 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

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3