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Reviewed, UniProtKB/Swiss-Prot Q2PQH8 (GDE_CANFA)

Last modified June 16, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycogen debranching enzyme
Alternative name(s):
    Glycogen debrancher
Including the following 2 domains:
    1- Recommended name:
            4-alpha-glucanotransferase
              EC=2.4.1.25
        Alternative name(s):
            Oligo-1,4-1,4-glucantransferase
    2- Recommended name:
            Amylo-alpha-1,6-glucosidase
                Short name=Amylo-1,6-glucosidase
              EC=3.2.1.33
        Alternative name(s):
            Dextrin 6-alpha-D-glucosidase
Gene names
Name: AGL
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length1533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation By similarity.

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the glycogen debranching enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15331533Glycogen debranching enzyme
PRO_0000232710

Regions

Region1 – ?4-alpha-glucanotransferase
Region? – 1533Amylo-1,6-glucosidase

Sites

Active site5271 By similarity
Active site5301 By similarity
Active site6281 By similarity

Amino acid modifications

Modified residue5851Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2PQH8-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 8A6E8A11F2252087

FASTA1,533174,828
        10         20         30         40         50         60 
MGHSKQIRIL LLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE 

        70         80         90        100        110        120 
KFRSLEWENP TEREDDSDKY CKLNLQQAGS FQYYFLQGNE KSGGGYIVVD PILYVGADNH 

       130        140        150        160        170        180 
VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SCYSLANQLE 

       190        200        210        220        230        240 
LNPDFSRPNK KYTWSDVGQL VEKMKKEWNV LCITDVVYNH TAANSKWIQE HPESAYNLVN 

       250        260        270        280        290        300 
SPHLKPAWVL DRALWHLSCD VAEGKYKEKG VPALIENDHQ MNCIRKIIWE DIFPKIQLWE 

       310        320        330        340        350        360 
FFQVDVYKAV EQFRRLLTQE NRKITTKPDP KEHLKIIQDP EYRRLGCTVD MNIALATFIP 

       370        380        390        400        410        420 
HDKGPAAIDE CCNWFRKRIE ELNSEKHQLV NYHQEQAVNC LLGNVFYERM AGHGPKLGPV 

       430        440        450        460        470        480 
TRKHPLVTRY FTFPFEEMTV STEESMIHNP NKACFLMAHN GWVMGDDPLR NFAEPGSEVY 

       490        500        510        520        530        540 
LRRELICWGD SVKLRYGNKP EDCPYLWAHM KKYTEITATY FQGVRLDNCH STPLHVAEYM 

       550        560        570        580        590        600 
LDAARKLQPN LYVVAELFTG SEDLDNIFVT RLGISSLIRE AMSAYNSHEE GRLVYRYGGE 

       610        620        630        640        650        660 
PVGSFVQPCL RPLMPAIAHA LFMDITHDNE CPIVHRSEYD ALPSTTIVSM ACCASGSTKG 

       670        680        690        700        710        720 
YDELVPHQIS VVSEERFYTK WNPGASPSNT GEVNFQSGII AARCAINKLH QELGAQGFIQ 

       730        740        750        760        770        780 
VYVDQVDEDI VAVTRHSPSI HQSVVSVSRT AFRNPKTSFY SKEVPQMCIP GKIEEVVLEA 

       790        800        810        820        830        840 
RTIERNTKPY QKDKNSINGM PNITVEIREH IQLSESKIVK QAGVATKGPN EYIQEIEFEN 

       850        860        870        880        890        900 
LSPGSVIIFR VSLDPHAQVA VGILRNHLTQ FSPHFKSGSL AVENSDPILK IPFAFIASKL 

       910        920        930        940        950        960 
TLAELNQVLY RCEAEEQEDG GGCYDIPNWS SLKYAGLQGL MSVLAEIRPK NDLGHPFCDN 

       970        980        990       1000       1010       1020 
LRSGDWMIDY VSNRLISRSG TIAEVGKWFQ AMFFYLKQIP RYLIPCYFDA ILIGAYTTLL 

      1030       1040       1050       1060       1070       1080 
DIAWKQMSSF VQNGSTFVKH LSLGSVQMCG VGKCPSLPLL SPSLMDVPYR LNEITKEKEQ 

      1090       1100       1110       1120       1130       1140 
CCVSLAAGLP HFSSGIFRCW GRDTFIALRG LLLITGRYLE ARNIILAFAG TLRHGLIPNL 

      1150       1160       1170       1180       1190       1200 
LGEGTYARYN CRDAVWWWLQ CIQDYCKMVP NGLDILKCPV SRMYPTDDSV PLSAGTLDQP 

      1210       1220       1230       1240       1250       1260 
LFEVIQEVMQ RHIQGIQFRE RNAGPQIDRN MKDEGFNITA GVDEETGFVY GGNRLNCGTW 

      1270       1280       1290       1300       1310       1320 
MDKMGESDRA RNRGIPATPR DGSAVEIVGL SKSTVRWLLE LSKKRIFPYH EVRVKRHGKV 

      1330       1340       1350       1360       1370       1380 
VTISYDEWNK KIQDNFEKLF HVSEDPXDFN EKHPNLVHKR GIYKDSYGAS SPWCDYQLRP 

      1390       1400       1410       1420       1430       1440 
NFTIAMVVAP ELFTAEKAWK ALEIAEKKLL GPLGMKTLDP DDMVYCGIYD NALDNDNYNL 

      1450       1460       1470       1480       1490       1500 
AKGFNYHQGP EWLWPVGYFL RAKLYFSKLM GPEANAKTVF LVKNILSRHY VHLERSPWKG 

      1510       1520       1530 
LPELTNENGQ YCPFSCETQA WSIATVLETL YDL 

« Hide

References

[1]"Glycogen storage disease type IIIa in curly-coated retrievers."
Gregory B.L., Shelton G.D., Bali D.S., Chen Y.T., Fyfe J.C.
J. Vet. Intern. Med. 21:40-46(2007) [PubMed: 17338148] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

DQ307574 mRNA. Translation: ABC25005.1.
RefSeqNP_001041561.1.
UniGeneCfa.18682

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Genome annotation databases

EnsemblENSCAFG00000020040. Canis familiaris. [Contig view]
GeneID479931.
KEGGcfa:479931.

Phylogenomic databases

HOVERGENQ2PQH8.

Enzyme and pathway databases

BRENDA2.4.1.25. 463.
3.2.1.33. 463.

Family and domain databases

InterProIPR010401. GDE_C.
IPR006421. Glyc_debranch.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10569. GDE_C. 1 hit.
PfamPF06202. GDE_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01531. glyc_debranch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGDE_CANFA
AccessionPrimary (citable) accession number: Q2PQH8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 24, 2006
Last modified: June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents