ID A0A151M4V6_ALLMI Unreviewed; 2015 AA.
AC A0A151M4V6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycogen debranching enzyme {ECO:0000256|ARBA:ARBA00020723};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE EC=3.2.1.33 {ECO:0000256|ARBA:ARBA00012778};
DE AltName: Full=Glycogen debrancher {ECO:0000256|ARBA:ARBA00031477};
GN Name=AGL {ECO:0000313|EMBL:KYO19547.1};
GN ORFNames=Y1Q_0007480 {ECO:0000313|EMBL:KYO19547.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO19547.1};
RN [1] {ECO:0000313|EMBL:KYO19547.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO19547.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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-glucosidase
CC in glycogen degradation. {ECO:0000256|ARBA:ARBA00003530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC Evidence={ECO:0000256|ARBA:ARBA00000927};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FRRS1 family.
CC {ECO:0000256|ARBA:ARBA00009195}.
CC -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC {ECO:0000256|ARBA:ARBA00025780}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO19547.1}.
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DR EMBL; AKHW03006584; KYO19547.1; -; Genomic_DNA.
DR STRING; 8496.A0A151M4V6; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR CDD; cd09628; DOMON_SDR_2_like; 1.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.4060; Reeler domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010401; AGL/Gdb1.
DR InterPro; IPR032788; AGL_central.
DR InterPro; IPR029436; AGL_euk_N.
DR InterPro; IPR032792; AGL_glucanoTrfase.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR032790; GDE_C.
DR InterPro; IPR006421; Glycogen_debranch_met.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR NCBIfam; TIGR01531; glyc_debranch; 1.
DR PANTHER; PTHR10569; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR10569:SF2; GLYCOGEN DEBRANCHING ENZYME; 1.
DR Pfam; PF03351; DOMON; 1.
DR Pfam; PF06202; GDE_C; 1.
DR Pfam; PF14701; hDGE_amylase; 1.
DR Pfam; PF14702; hGDE_central; 1.
DR Pfam; PF14699; hGDE_N; 1.
DR Pfam; PF02014; Reeler; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS50836; DOMON; 1.
DR PROSITE; PS51019; REELIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 1904..1924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1945..1970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1976..1997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1569..1730
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 1747..1863
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 1867..2015
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT REGION 1528..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2015 AA; 225926 MW; 07CFE090D2FB70C1 CRC64;
MPHGKQTRVL HLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKHVTVYTNY PASGEIFDRH
KFRPLSWHNP TGREDDSDKY CKLDLQISGS YQYYFSLEHE KSGGGYVVVD PILRVGADNH
VLPLDCVTLQ TFLAKCLGPF YEWEDRLKVA KESGYNMIHL TPVQKLGRSR SSYSLADQLE
VNPDFSSPNY KCTWSDVGKL VEKMKNEWNM LCITDVVYNH TAANSEWLKV HPECSYNLVN
SPHLKPAWVL DRALWHLTCS VAGGKCTDRG VPPSIENDHH LNCIRKIIWE DLYPRTKLWE
FFQVDVNKAV QQFKTLLTQG TKNTKSDPNK HLKIIQDPKY RRLGCTVDMD TALATFIPHS
NGPAAIEECC NWFRERIEEL NAEQFRQVNH HQEQAVNCLV GNVVYERLAD HGPKLGPVTR
KYPLVTRYFT YPFEDQTLEE EELLMHQSDK ACHFMAHNGW VMGDDPLKNF AEPGSNVYLR
RELICWGDSV KLRYGKKPED CPYLWAHMKK YTEITAKYFH GIRLDNCHST PIHVAEYMLD
TARKLRADFY IVAELFTGSE ELDNIFVNTL GINSLIREAM SAYNSHEEGR LVYRFGGEPV
GSFVQPRLRP LMPAIAHALF MDITHDNECP IQHRSAYDAL PSSMIVSMAS CATGSTRGYD
ELVPHQISVV SEERFYAKWN PSATPLTPGE VNFQTGIIGG RLAMNRLHQE LAIKGFIQVY
VDQVDEDIVA VTRHCPNTHQ SVVAVSRTAF RDPKTSFYSK EVPEMCIPGI IEEVVLEART
VERNVSPYEK DEHAINGLPN YTVEIREHIQ IKESKIIKQA GTAIKGPNEF VQEIEFENLT
PGSVIIFRVS LDPKAQEAVG VLRNHLIQFS PHFKSGSLPD DHSAPILKTL FSFIASKLTL
ADLNQVLYRC DAEEQEDGGG CYNIPNWSPL KYAGLQGLIS VMADIRPKND LGHPFCDNLR
SGDWMIDYVS DRLISRAGAC AEVGIWLKAM FIYLKQIPRY LIPCYFDAIL VGAYTTLLDV
AWCQMSSFVQ NGSTFVKHLA LGSVQMCGIG KYPCLPNLSP TLQDVPYRVN EITEQKEQCC
VTLAAGLPHF SSGIFRCWGR DTFIALRGLM LVTGRHLEAR NIILAFAGTL RHGLIPNLLG
QGTHARYNCR DAVWWWLQCI QDYCKIVPNG TDILMCPVSR TYPKDDSSPQ SAGTLDQPLY
EVIQEAMQRH MEGIQFRERN AGPQIDRNMR DEGFNVTAGI NQETGFVCGG NRFNCGTWMD
KMGESERARN KGIPATPRDG SAVEIVGLCK STVRWLLELS KKNEFPYHGV TVKRHGKEET
ITYDEWNRKI QGHFEKLFFV SENPSDPSEK YPNLVHKRGI YKDSYGASSP WCDYQLRPNF
TIAMVVAPEM FTPERAWKAL EVAEKKLLGP LGMKTLDPDD MVYCGIYDNA LDNDNYNVAR
GFNYHQGPEW LWPIGYFLRA KLYFSKLIGP EIYAKTVFLV KNVLSRHYVH LERSSWKGLP
ELTNENGQYC PFSCESQAWS IAVILETGAA PSSPPRPAPR PEQPPRREVG RSQMEVWVFW
LLLFCGVFSG EVLGFPNGGV TSACDSMPPG HGSSVPQTTS APYYISVSNT SFGPGDKIIV
TLQANDSSSF KGFLLQTRTI LGDVAVGTFH IIDANTQGLL CNKILNSSLS QTNPESKKII
RAIRVAPADI GNVEFRATVV QSLNVFWTDV KSQTLISSSH PTPVTSGHVG CGTKKFCFSS
PAGCNLDDPS CYFMSSEEEG GDAFKFEMSG LSDGYISIGF SDDMQMGNDD IYICTKNSAG
RIEVQHAFST GRTTPEILPL GDVQNTVTSF NNGIIKCSFT TKNAMSTHLK AAGTSYFIFL
AVGPSVSGQI QKHSKIPFIT NEKVNISSYM AVGGTSSTPS IIKAHGALML IAWMTTGSMG
MLFARNVKKA SHSLLLGKAV WFQVHWCLMA LTVAKTTTAF ILAFVAAMGW SNGAGAHAII
GCIVMILSFF QPVIAFLQPS LQNKSCCHIF GPTDA
//
