ID A0A077YY01_TRITR Unreviewed; 689 AA.
AC A0A077YY01;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=TTRE_0000127001 {ECO:0000313|EMBL:CDW53007.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW53007.1};
RN [1] {ECO:0000313|EMBL:CDW53007.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW53007.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; HG805838; CDW53007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077YY01; -.
DR STRING; 36087.A0A077YY01; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 202..572
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 397
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 689 AA; 79856 MW; 6D4698E330BBD055 CRC64;
MDVLGSERLR PPEFNNLLKF DGYLHNFESE ISRRYGIFRN ALERIDKNEG GLDKFTRGYE
TFGMIVTPAN GVVCREWAPG ADGLFLRGDF NGWSRTSHPY DRKEFGRWEL YIPPKDDGSC
PIPHGSVLKV LVTKDGHIYD KVSPWATYVC CPSDSIIYHQ VFYNPPEKYQ FKYARPSEPR
ALRIYESHVG ISSIEGKVAD YRHFADNVIP RIDKQGYNTI QLMAVMEHAY YASFGYQVTS
FFAASSRYGP PDDLKYLVDK AHERDIIVLL DIVHSHACKN TADGLNQWDG TNGCYFHNNA
RGFHDLWDSR LFNYTETEVL RFLLSNLRWW IEEYHFDGFR FDGVTSMIYH SHGLGHGFSG
DYNEYFNLNA DTDSLVYLML ANYSMKKIYP HIITIAEEVS GLPALCRPVE EGGLGFDYRL
AMAIPDKWIE LLKEKRDEEW KMGDIVFTME NRRYGEKCIA YAESHDQALV GDKTIAFWLM
DKEMYDFMST ITPLTPIIER GLALHKMIRL ITHALGGEGW LNFMGNEFGH PEWLDFPRAG
NNVSYHYCRR QWNLVDDDLL RYKFLNNWDR AMNMAEEKYH WLSSGPGFTS WKHEDDKVIA
FERGGVLFVF NFHCSKSFPD YKVGVARPGK YKLVLNSDAS EFGGQNRLDP NSRHLTFPYE
YAGRPHHLLV YVPSRVCIAL APEDEKEEQ
//
