ID A0A0V1PMA4_9BILA Unreviewed; 1455 AA.
AC A0A0V1PMA4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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|EMBL:KRZ97341.1};
GN ORFNames=T08_15173 {ECO:0000313|EMBL:KRZ97341.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ97341.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ97341.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ97341.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
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:KRZ97341.1}.
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DR EMBL; JYDM01000003; KRZ97341.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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:0005975; P:carbohydrate metabolic 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; IPR025946; CABIT_dom.
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; PF12736; CABIT; 1.
DR Pfam; PF02922; CBM_48; 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 Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 972..1340
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 48..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 163371 MW; 8FA82497327BA10F CRC64;
MQFVNQNVPS TVIVRCLDKL MINGNISHFD GDSVDLDFRG SGVKRQRSDG WLVGRSGGRP
SANRNEQPIR EQVLPTTGPV DNGRQTQPPG PVDQSVRFRA DRPSVSRLAR ALSKWESTDD
AGKKRKFPSP DSGLVEKRPT NGVIVDKLAG WSRTMRVTAE TPLLTTVKWD VENAPFLNEF
VDRYPLPHVA LVTKGQHLGV GLPNVSNPTL KPYLLAYAKQ RSRKLLGTLV KIKDGKRSAL
SAASVAIPLE YGGYFEILSE DGHRPPCFET VGELAAHTSV DQCLVRQRCK AYLPDADGEL
KTLRRSRAVL PGEVLTVVGQ FRLKRVWFLR CFDEAGRSLF FKAHHKGRFS ALAKAESVGG
VHTAASLASK RLPLTVRLVH GHCPAEVAKL AGSAELIIRL RSVYEEQFLL AYCLQKSEGQ
LLSIPLNAHL KLAPAVNYPQ MVVHPEFRQL CAYCAKLAPS FSNRLSLLHQ PDQLTARASA
FHINDADENS SGGGSWCRSR SRSGSRSGSG SWSAATVDQD EHELQALYDC IRAAPTRNGD
GDRSWSSRLV VERPTMVDDW PDAGRRQLCY HCHCTDGSAC DSTPPPPPPP QPLPPPPTLP
LQPPQPLPLP LLLSATTATT TAAAAAAAVT PRRRHTAARP RPKSLFLPDT SRFFYPIAPF
TSPSTPVYSK PRRPTGCELT TVAQPYHSAF TTTYRPPPYP AYAAVYTAYE VLFFCVLTSG
SVVMGSVFSS IGDAFSSLCE GFNAIFAEIG KIPEYCGCLR GLSEVENIDI IMSDRPPSLN
NLLQLDGYLK NYENEICRRY GEFKRLVMQI NKEEGGLDKF SRGYEIFGVV VTPENGVFCQ
EWAPGADGLF LIGDFNNWDR TAHPYDRKDF GKWELYIPPN ADGSCPIPHK SVLKIMVAKD
GGFCDKISPW ATYVCCPSDS VVYHHVFYNP PQKYKFLYNK PEKPVALRIY ECHIGISSPE
GKVASYVYFT NNIIPRIVKQ GYNAIQVMAV MEHAYYASFG YQVTNFFAAS SRYGTPCDLK
FLVDKAHELG IFVLLDIVHS HASKNTADGL NQWDGTNGCY FHDNYRGYHT VWDSRLFNYS
ERETLRFLLS NLRWWIEEYH FDGFRFDGVT SMIYHSHGLG TGFSGHYDEY FGLSVDTESL
LYLTTANYML HTFYPSVVTI AEEVSGMPAL CRPVEEGGQG FDYRLAMAIP DKWIKLLKHY
RDEDWNMGDL VFTLENRRYG EKNIAYAESH DQALVGDKTI AFWLMDKEMY TDMSTLCPLN
STIDRGIALH KMIRLITHGL GGEGLIIAEH IAGNEFGHPE WLDFPRQGNN SSYHYCRRQW
NLVDDPLLRY KFLNNWDRAM NLAEEKYHWL SAGPAYTSWK HDQDKVIAFE RANLLFVFNF
HVNKSYTDYK IGVNKSGKYK MILDSDAEEF GGHQRLDSSC EWFTFPHEYA NRANHLCVYA
PSRCCFVLAL DSDLS
//
