ID A0A090LKZ3_STRRB Unreviewed; 676 AA.
AC A0A090LKZ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=SRAE_2000501800 {ECO:0000313|EMBL:CEF70385.1,
GN ECO:0000313|WBParaSite:SRAE_2000501800.1,
GN ECO:0000313|WormBase:SRAE_2000501800};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF70385.1};
RN [1] {ECO:0000313|EMBL:CEF70385.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000501800.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF70385.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000501800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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 EMBL; LN609529; CEF70385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LKZ3; -.
DR STRING; 34506.A0A090LKZ3; -.
DR EnsemblMetazoa; SRAE_2000501800.1; SRAE_2000501800.1; WBGene00265269.
DR WBParaSite; SRAE_2000501800.1; SRAE_2000501800.1; WBGene00265269.
DR WormBase; SRAE_2000501800; SRP10510; WBGene00265269; -.
DR eggNOG; KOG0470; Eukaryota.
DR OMA; YEMHLGS; -.
DR OrthoDB; 96at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 190..564
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 676 AA; 79148 MW; A23D723C41F97542 CRC64;
MIPTKLDDLF NDDEYLKPFK NEIVRRYNAF QDGLKAIDNC GGLDDFTKGY KHYGIIVKDD
NSIFCREWAP GADGLSLVGD FNNWNKESHK YVRKDFGKWE LEIAPDSDGN CLIKHDSHLK
IVVWKNGVPH FKLSPWANYV KQYEKEVVFH QRFWNPKEKF EFKHPHPPKP ESLRIYEAHV
GISSYEEKVN TYIDFADNVL PRIKNQGYNT IQLMAIMEHA YYASFGYQVT SFFAPSSRFG
TPDDLKYLVD KAHSMGITML LDVVHSHASK NIEDGLNEWD CTNSCYFHGN ARGYHTLWDS
RLFDYTQIEV QRFLLSNLRY WVEEYGFDGF RFDGVTSMIY HNHGMNESFA GGYPMYFGMN
VDTESLLYIT IANYMLHKFY PKYMITIAEE VSGMPALCRE IEEGGQGFDY RLAMAIPDLW
IKILKHTRDE DWKIGEIVFQ LENRRYKEKH VTYAESHDQA LVGDKTIAFW LMDKEMYTNM
SCISENTHII DRGIALHKLI RLITYGLGGE AWLNFIGNEF GHPEWLDFPR AGNNSSYKYA
RRQWNIVDDE LLRYKFLNNW DRSMNQLEES FHFLSRGYAY VSWKHDDDKV VAFERAGLVW
IINFHPSKSF TDYKIGVEVS GCYQIALNSD EEKYGGHNRL DMDQKIFTFP EGYAGRRNHI
CVYIPSRVGI VLKKID
//
