ID A0A401SPL0_CHIPU Unreviewed; 698 AA.
AC A0A401SPL0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=chiPu_0010800 {ECO:0000313|EMBL:GCC32339.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC32339.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC32339.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- 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:GCC32339.1}.
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DR EMBL; BEZZ01000427; GCC32339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SPL0; -.
DR STRING; 137246.A0A401SPL0; -.
DR OMA; YEMHLGS; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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:UP000287033};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 145..532
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 376
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 698 AA; 80452 MW; BEC98BBC8313122A CRC64;
MEGASYEERL SRYNKFVSLA RSIEENEGSL EQFSRSYETF GVNRLADGGI YCKEWAPGAN
SVSLVGEFNG WNSSSHCYKM LPFGKWELYI PPRADGSSPI AHGSKLKVVM VCKTGQQLYR
ISPWARYVIR EQNSSTYEWV HWDPPRRYER KYPHPPRPNS VRIYEAHVGI ASPEGKIASY
KNFTHNMLVR IKKLGYNCIQ LMAVMEHAYY ASFGYQVTSF FAASSRFGTP DELKELVDTA
HSMGLFVLLD VVHSHASKNT QDGLNLFDGT DDCFFHSGAR GTHLLWDSRL FNYSNWEVLR
FLLSNLRWWV EEYYFDGFRF DGVTSMLYHH HGISTSFSGN YSEYFGLQVD EDSFVYLMLS
NYMLHSFYPD FITVAEDVSG MPTLCRPMIE GGGGFDYRLA MAIPDKWIQI LKELKDEDWN
MGNIIYTLTN RRYGEKCIAY AESHDQALVG DKTLAFWLMD AEMYTNMSVL TPFTVVVDRG
IQLHKMIRLI THALGGEGYL NFIGNEFGHP EWLDFPRIGN NESYHYARRQ FDLLDNHLLR
YQQLNAFDAD MNNLEEKYGW LAAPPAYVSE KHEGNKVIAF ERANLLFIFN FNPEKSFPDY
RVGIDRPGKY KIVLDTDSTD YGGHGRLNHN TEFFTDAQIQ NDRPNSVLFR SDDSDFSLRR
GHAAELVGYG TLHCCENSFK VYIPSRTAII LANMDIHK
//
