ID H2LDN8_ORYLA Unreviewed; 655 AA.
AC H2LDN8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 67.
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:ENSORLP00000004049.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000004049.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000004049.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000004049.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000004049.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000004049.2};
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}.
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DR AlphaFoldDB; H2LDN8; -.
DR Ensembl; ENSORLT00000004050.2; ENSORLP00000004049.2; ENSORLG00000003252.2.
DR eggNOG; KOG0470; Eukaryota.
DR GeneTree; ENSGT00390000017040; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR TreeFam; TF300783; -.
DR Proteomes; UP000001038; Chromosome 13.
DR Bgee; ENSORLG00000003252; Expressed in liver and 14 other cell types or tissues.
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:UP000001038};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 154..536
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 317
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 372
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 655 AA; 75965 MW; 26F48DB3BB9BC235 CRC64;
QRCFFLHWHE HLQKLLFQLE ETEGGFDQFT RSYRSFGVQR QPDNSLFFKE WAPGAEALFL
TGDFNDWNKF SHPYAKKEFG KWELILPPKH DGSPAVDHNS KLKVVVHTND GQRIYRISPW
AKYVAREGKA VIYDWVHWDP PHPYIHIHPR PKKPTSLRIY EAHVGIASPE PKVASYSNFT
TNVLPRIKDL GYNCIQLMAI MEHVYYACFG YQITSYFAAS SRYGTPDELK QLIDVAHSMG
IVVLLDVVHS HASKNTEDGL NRFDGTDSCF FHSPPRGEHS LWDSRLFNYS SWEVLRFLLS
NLRWWMEEYR FDGFRFDGVT SMLYHHHGIG TGFSGDYNEY FGLHVDEDSL VYLMLANHIL
HTLYPDCITI AEDVSGMPAL CRGVQEGGLG FDYRLAMAIP DKWIQILKEL KDEDWNMGDI
AFTLTNRRYG EKCIAYAESH DQALVGDKTL AFWLMDKEMY TNMSTLIPMS PIIDRGIQLH
KMIRLLTHGL GGEGYLNFIG NEFGHPEWLD FPREGNNQSY HYARRQFNLL DTDHLRYCQL
YAFDRDMNRA EDKYGWLAAP PAFVSAKHEG DKVIVFDRAN VLFIFNFHPN RSFQDYRVGV
EAAGKYKIKL DSDEVQYGGH GRLDHSTDFF TEPHPFNGRS NSMLVNISNM TFLTH
//
