ID   GDE_CANFA               Reviewed;        1533 AA.
AC   Q2PQH8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Glycogen debranching enzyme;
DE   AltName: Full=Glycogen debrancher;
DE   Includes:
DE     RecName: Full=4-alpha-glucanotransferase;
DE              EC=2.4.1.25;
DE     AltName: Full=Oligo-1,4-1,4-glucantransferase;
DE   Includes:
DE     RecName: Full=Amylo-alpha-1,6-glucosidase;
DE              Short=Amylo-1,6-glucosidase;
DE              EC=3.2.1.33;
DE     AltName: Full=Dextrin 6-alpha-D-glucosidase;
GN   Name=AGL;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17338148; DOI=10.1892/0891-6640(2007)21[40:GSDTII]2.0.CO;2;
RA   Gregory B.L., Shelton G.D., Bali D.S., Chen Y.T., Fyfe J.C.;
RT   "Glycogen storage disease type IIIa in curly-coated retrievers.";
RL   J. Vet. Intern. Med. 21:40-46(2007).
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-
CC       glucosidase in glycogen degradation (By similarity).
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       to a new position in an acceptor, which may be glucose or a
CC       (1->4)-alpha-D-glucan.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->6)-alpha-D-glucosidic branch
CC       linkages in glycogen phosphorylase limit dextrin.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
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DR   EMBL; DQ307574; ABC25005.1; -; mRNA.
DR   RefSeq; NP_001041561.1; -.
DR   UniGene; Cfa.18682; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   Ensembl; ENSCAFG00000020040; Canis familiaris.
DR   GeneID; 479931; -.
DR   KEGG; cfa:479931; -.
DR   HOVERGEN; Q2PQH8; -.
DR   BRENDA; 2.4.1.25; 463.
DR   BRENDA; 3.2.1.33; 463.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EC.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010401; GDE_C.
DR   InterPro; IPR006421; Glyc_debranch.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   PANTHER; PTHR10569; GDE_C; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   TIGRFAMs; TIGR01531; glyc_debranch; 1.
PE   2: Evidence at transcript level;
KW   Glycogen biosynthesis; Glycogen storage disease; Glycosidase;
KW   Glycosyltransferase; Hydrolase; Multifunctional enzyme;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1   1533       Glycogen debranching enzyme.
FT                                /FTId=PRO_0000232710.
FT   REGION        1      ?       4-alpha-glucanotransferase.
FT   REGION        ?   1533       Amylo-1,6-glucosidase.
FT   ACT_SITE    527    527       By similarity.
FT   ACT_SITE    530    530       By similarity.
FT   ACT_SITE    628    628       By similarity.
FT   MOD_RES     585    585       Phosphotyrosine (By similarity).
SQ   SEQUENCE   1533 AA;  174828 MW;  8A6E8A11F2252087 CRC64;
     MGHSKQIRIL LLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE
     KFRSLEWENP TEREDDSDKY CKLNLQQAGS FQYYFLQGNE KSGGGYIVVD PILYVGADNH
     VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SCYSLANQLE
     LNPDFSRPNK KYTWSDVGQL VEKMKKEWNV LCITDVVYNH TAANSKWIQE HPESAYNLVN
     SPHLKPAWVL DRALWHLSCD VAEGKYKEKG VPALIENDHQ MNCIRKIIWE DIFPKIQLWE
     FFQVDVYKAV EQFRRLLTQE NRKITTKPDP KEHLKIIQDP EYRRLGCTVD MNIALATFIP
     HDKGPAAIDE CCNWFRKRIE ELNSEKHQLV NYHQEQAVNC LLGNVFYERM AGHGPKLGPV
     TRKHPLVTRY FTFPFEEMTV STEESMIHNP NKACFLMAHN GWVMGDDPLR NFAEPGSEVY
     LRRELICWGD SVKLRYGNKP EDCPYLWAHM KKYTEITATY FQGVRLDNCH STPLHVAEYM
     LDAARKLQPN LYVVAELFTG SEDLDNIFVT RLGISSLIRE AMSAYNSHEE GRLVYRYGGE
     PVGSFVQPCL RPLMPAIAHA LFMDITHDNE CPIVHRSEYD ALPSTTIVSM ACCASGSTKG
     YDELVPHQIS VVSEERFYTK WNPGASPSNT GEVNFQSGII AARCAINKLH QELGAQGFIQ
     VYVDQVDEDI VAVTRHSPSI HQSVVSVSRT AFRNPKTSFY SKEVPQMCIP GKIEEVVLEA
     RTIERNTKPY QKDKNSINGM PNITVEIREH IQLSESKIVK QAGVATKGPN EYIQEIEFEN
     LSPGSVIIFR VSLDPHAQVA VGILRNHLTQ FSPHFKSGSL AVENSDPILK IPFAFIASKL
     TLAELNQVLY RCEAEEQEDG GGCYDIPNWS SLKYAGLQGL MSVLAEIRPK NDLGHPFCDN
     LRSGDWMIDY VSNRLISRSG TIAEVGKWFQ AMFFYLKQIP RYLIPCYFDA ILIGAYTTLL
     DIAWKQMSSF VQNGSTFVKH LSLGSVQMCG VGKCPSLPLL SPSLMDVPYR LNEITKEKEQ
     CCVSLAAGLP HFSSGIFRCW GRDTFIALRG LLLITGRYLE ARNIILAFAG TLRHGLIPNL
     LGEGTYARYN CRDAVWWWLQ CIQDYCKMVP NGLDILKCPV SRMYPTDDSV PLSAGTLDQP
     LFEVIQEVMQ RHIQGIQFRE RNAGPQIDRN MKDEGFNITA GVDEETGFVY GGNRLNCGTW
     MDKMGESDRA RNRGIPATPR DGSAVEIVGL SKSTVRWLLE LSKKRIFPYH EVRVKRHGKV
     VTISYDEWNK KIQDNFEKLF HVSEDPXDFN EKHPNLVHKR GIYKDSYGAS SPWCDYQLRP
     NFTIAMVVAP ELFTAEKAWK ALEIAEKKLL GPLGMKTLDP DDMVYCGIYD NALDNDNYNL
     AKGFNYHQGP EWLWPVGYFL RAKLYFSKLM GPEANAKTVF LVKNILSRHY VHLERSPWKG
     LPELTNENGQ YCPFSCETQA WSIATVLETL YDL
//