ID H0ZTJ1_TAEGU Unreviewed; 700 AA.
AC H0ZTJ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN Name=GBE1 {ECO:0000313|Ensembl:ENSTGUP00000013937.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000013937.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000013937.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000013937.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000826};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H0ZTJ1; -.
DR STRING; 59729.ENSTGUP00000027926; -.
DR Ensembl; ENSTGUT00000014096.2; ENSTGUP00000013937.2; ENSTGUG00000013536.2.
DR GeneTree; ENSGT00390000017040; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR OrthoDB; 96at2759; -.
DR TreeFam; TF300783; -.
DR Proteomes; UP000007754; Chromosome 1.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 192..508
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 394
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 700 AA; 80810 MW; EE8B0E774F43BC68 CRC64;
MAAASTEPPR LKQLLERDPY LAPFRTDFQR RYSLFYNRLK NIEESEGGLD KFTKSYKTFG
VNQLADGGIY CKEWAPGAEA VFLAGDFNGW NPSSHPYKKL EYGKWELFIP PEDGHSPVPH
GSKLKVVIRA QNGALLYRIS PWARYVVRDE DKVNYDWVHW NPPQSYIHKN PSPKRLKSLR
IYESHVGIAS PEGKVASYKN FTYNVLPRIK DLGYNCVQLM AIMEHAYYAS FGYQVTSFFA
ASSRYGTPDD LKEMIDVAHS MGITVLLDVV HSHASKNSED GLNQFDGTDS CFFHSGYRGN
HQLWDSRLFD YANWEVLRFL LSNLRMWIED YRFDGFRFDG VTSMLYHHHG IGTGFSGDYN
EYFGLHVDED ALCYLMLANH MINTLHPECI TIAEDVSGMP ALCRPVAEGG GGFDYRLAMA
IPDKWIQIIK ELKDEDWNMG NIVHTLTNRR CEEKYIAYAE SHDQALVGDK TLAFRLMDAE
MYTNMSVLMP LTPVIDRGIQ LHKMIRLITH ALGGESYLNF MGNEFGHPEW LDFPRIGNNE
SYHYARRQFN LTEDDLLRYK FLNAFDRDMN KLEERYGWLA SPQAYVSEKH ESNKVIAFER
AGLIFIFNFH PYQSYVDYRV GIETPGKYKI LLDSDAGEYG GHQRLDHNTE YFSEEYPHNY
RPNSIMSSSS QPPRGCQLHQ IKVYIPSRVA LVLHTMDIPK
//
