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Protein

Glycogen debranching enzyme

Gene

AGL

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei549 – 5491By similarity
Active sitei552 – 5521By similarity
Active sitei650 – 6501By similarity

GO - Molecular functioni

  1. 4-alpha-glucanotransferase activity Source: UniProtKB-EC
  2. amylo-alpha-1,6-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB-KW
  2. glycogen catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Glycosyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen debranching enzyme
Alternative name(s):
Glycogen debrancher
Including the following 2 domains:
4-alpha-glucanotransferase (EC:2.4.1.25)
Alternative name(s):
Oligo-1,4-1,4-glucantransferase
Amylo-alpha-1,6-glucosidase (EC:3.2.1.33)
Short name:
Amylo-1,6-glucosidase
Alternative name(s):
Dextrin 6-alpha-D-glucosidase
Gene namesi
Name:AGL
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

  1. Cytoplasm By similarity

  2. Note: Under glycogenolytic conditions localizes to the nucleus.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15551555Glycogen debranching enzymePRO_0000087451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871PhosphoserineBy similarity

Post-translational modificationi

The N-terminus is blocked.
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Monomer. Interacts with NHLRC1/malin (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008168.

Structurei

3D structure databases

ProteinModelPortaliP35574.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1555Amylo-1,6-glucosidase
Regioni1 – ?4-alpha-glucanotransferase

Sequence similaritiesi

Belongs to the glycogen debranching enzyme family.Curated

Phylogenomic databases

eggNOGiCOG3408.
HOGENOMiHOG000212981.
HOVERGENiHBG005824.
InParanoidiP35574.
KOiK01196.

Family and domain databases

Gene3Di3.20.20.80. 5 hits.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR010401. AGL/Gdb1.
IPR029436. AGL_euk_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR006421. Glycogen_debranch_met.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10569. PTHR10569. 1 hit.
PfamiPF06202. GDE_C. 1 hit.
PF14699. hGDE_N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR01531. glyc_debranch. 1 hit.

Sequencei

Sequence statusi: Complete.

P35574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSFDFGVL LILLKYFKSS RSQNGHSKQI RILLLNEMEK LEKTLFRLEQ
60 70 80 90 100
GFELQFRLGP TLQGKPVTVF TNYPFPGETF NREKFRSLEW ENPTEREDDS
110 120 130 140 150
DKYCKLNLQQ SGSFQYYFLQ GNEKSGGGYI VVDPILRVGA DNHMLHLDCV
160 170 180 190 200
TLQTFLAKCL GPFDEWESRL RVAKESGYNM IHFTPLQTLG LSRSCYSLAD
210 220 230 240 250
QLELNPDFSR PHKKYTWSDV GQLVEKLKRE WNVLCITDVV YNHTAANSKW
260 270 280 290 300
IQEHPECAYN LVNSPHLKPA WVLDRALWHF SCDVAEGKYK NRGVPALIEN
310 320 330 340 350
DHHLNCIRKV IWEDIFPKLH LWEFFQVDVY KAVEKFRGLL TQETWRVIKS
360 370 380 390 400
DPKQHLKIIQ DPEYRRFGCT VDMNIALATF IPHDNGPAAI EECCNWFRKR
410 420 430 440 450
IEELNSEKHQ LMNYHQEQAV NCLLGNVFYE RLAGHGPKLG PVTRKYPLVT
460 470 480 490 500
RYFTFPFEEM PVSTEETMIH LPNKACFFMA HNGWVMGDDP LRNFAEPGSD
510 520 530 540 550
VYLRRELICW GDSVKLRYGT KPEDCPYLWA HMRKYTEIIA TYFQGVRLDN
560 570 580 590 600
CHSTPLHVAE YMLDAARKLQ PNLYVVAELF TGSEDLDNIF VTRLGISSLI
610 620 630 640 650
REAMSAYNSH EEGRLVYRYG GEPVGSFVQP CLRPLMPAIA HALFMDITHD
660 670 680 690 700
NECPIVHRSV YDALPSTTIV SMACCASGST RGYDELVPHQ ISVVSEERFY
710 720 730 740 750
TKWNPEALPS NAGEVNFQSG IIAARCAINK LHQELGAKGF IQVYVDQVDE
760 770 780 790 800
DIVAVTRHSP SIHQSFVAVS RTAFRNPKTS FYSKDVPQMC IPGKIEEVVL
810 820 830 840 850
EARTIERNIS PYRKDENSIN GMPNITVEIR EHIQLNESRI VKQAGVTTKG
860 870 880 890 900
PNEYIQEIEF ENLSPGSVII FRVSLDPHAQ VAVGILRNHL TQFSAHFKAG
910 920 930 940 950
SLAVDNSDPI LKIPFASIAS KLTLAEINQI LYRCESEEQE DGGGCYDIPN
960 970 980 990 1000
WSSLKYAGLQ GLMSVLAEIR PKNDLGHPFC DNLRSGDWMI DYVSGRLISR
1010 1020 1030 1040 1050
SGTIAEVGKW LQAMFFYLKQ IPRYLIPCYF DAILIGAYTT LLDIAWKQMS
1060 1070 1080 1090 1100
SFVQTGSTFV KHLSLGSVQM CGVGKFPSLP LLSPSLTDVP YRLNEITKEK
1110 1120 1130 1140 1150
EQCCVSLAAG LPHFSSGIFR CWGRDTFIAL RGLLLITGRY LEARNIILAF
1160 1170 1180 1190 1200
AGTLRHGLIP NLLGEGTYAR YNCRDAVWWW LQCIQDYCKM VPNGLDILKC
1210 1220 1230 1240 1250
PVSRMYPTDD SAPLPAGTLD QPLFDVIQEA MQRHMQGIQF RERNAGPQID
1260 1270 1280 1290 1300
RNMKDEGFTV IAGVNEETGF VYGGNRFNCG TWMDKMGESD RARNRGIPAT
1310 1320 1330 1340 1350
PRDGSAVEIV GLCKSTVRWL LELSKKNIFP YHEVRVKRHG KVVTVSYEEW
1360 1370 1380 1390 1400
NRKIQDNFEK RFHVSEDPSA SNEEHPNLVH KRGIYKDSYG ASSPWCDYQL
1410 1420 1430 1440 1450
RPNFTIAMVV APELFTAEKA WKALEIAEKK LLGPLGMKTL DPDDMVYCGI
1460 1470 1480 1490 1500
YDNALDNDNY NLAKGFNYHQ GPEWLWPVGY FLRAKLYFSK LMDRETNART
1510 1520 1530 1540 1550
IFLVKNVLSR HYVHLERSPW KGLPELTNEN GQYCPFSCET QAWSIATILE

TLYDL
Length:1,555
Mass (Da):177,656
Last modified:June 1, 1994 - v1
Checksum:i7AD214297CB966E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10605 mRNA. Translation: AAA16364.1.
PIRiS38758.
RefSeqiNP_001075716.1. NM_001082247.1.
UniGeneiOcu.1807.

Genome annotation databases

GeneIDi100009066.
KEGGiocu:100009066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10605 mRNA. Translation: AAA16364.1.
PIRiS38758.
RefSeqiNP_001075716.1. NM_001082247.1.
UniGeneiOcu.1807.

3D structure databases

ProteinModelPortaliP35574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008168.

Chemistry

BindingDBiP35574.
ChEMBLiCHEMBL5273.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009066.
KEGGiocu:100009066.

Organism-specific databases

CTDi178.

Phylogenomic databases

eggNOGiCOG3408.
HOGENOMiHOG000212981.
HOVERGENiHBG005824.
InParanoidiP35574.
KOiK01196.

Miscellaneous databases

PROiP35574.

Family and domain databases

Gene3Di3.20.20.80. 5 hits.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR010401. AGL/Gdb1.
IPR029436. AGL_euk_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR006421. Glycogen_debranch_met.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10569. PTHR10569. 1 hit.
PfamiPF06202. GDE_C. 1 hit.
PF14699. hGDE_N. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR01531. glyc_debranch. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, sequencing, and analysis of the cDNA for rabbit muscle glycogen debranching enzyme."
    Liu W., de Castro M.L., Takrama J., Bilous P.T., Vinayagamoorthy T., Madsen N.B., Bleackley R.C.
    Arch. Biochem. Biophys. 306:232-239(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Muscle.

Entry informationi

Entry nameiGDE_RABIT
AccessioniPrimary (citable) accession number: P35574
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 29, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.