ID U6KZC7_EIMTE Unreviewed; 1016 AA.
AC U6KZC7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ETH_00002275 {ECO:0000313|EMBL:CDJ43321.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ43321.1};
RN [1] {ECO:0000313|EMBL:CDJ43321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ43321.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ43321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ43321.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; HG675759; CDJ43321.1; -; Genomic_DNA.
DR RefSeq; XP_013234071.1; XM_013378617.1.
DR AlphaFoldDB; U6KZC7; -.
DR EnsemblProtists; CDJ43321; CDJ43321; ETH_00002275.
DR GeneID; 25249670; -.
DR VEuPathDB; ToxoDB:ETH2_1017800; -.
DR VEuPathDB; ToxoDB:ETH_00002275; -.
DR OMA; ERYKFEI; -.
DR OrthoDB; 211317at2759; -.
DR UniPathway; UPA00164; -.
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:UniProtKB-UniPathway.
DR CDD; cd11322; AmyAc_Glg_BE; 1.
DR CDD; cd02855; E_set_GBE_prok_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; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
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 NCBIfam; TIGR01515; branching_enzym; 1.
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 SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 478..864
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 115145 MW; CFF6A51A4C33D145 CRC64;
MADSTQAQAQ EFGRRKGPTS SSKATEEVSS PSCFRHPSQD PAGTETRDSP TMEALTTQLN
EAVRISGTDS LVAQDKSRLD LHPTKQGTTA FDSCSTNGAS LTYEEKQHRT EDGVAPPRAI
ERTTACTSGY IPTSGPKEQP YTNMNDVAKV DHVEEAQRHD QTHFMAVPID VLPPNADIPE
YDMHLLNLAR HADPFRMLGC HKVECADSDK RIVVVRVWLK NVDHVELRPR AGVSDWRLPP
PLESVQLERK GELLFHKASA NARAASAFEM YTTDPSASSR GCPVKSSDPY VPLDYELLVR
GEGEETPRVV YDTYSFGMTV PQYNLELFQS GSCWHVDNLM GSHIITVDGV TGVRFAVWAP
NCICVSVVGD WNGWDGRAHP MRKRVEFGCW DLFIPGIGAG EKYGYRIHAR NGTDFIKIDP
YAQEFEVPPK TASIISACDD AFKPAESRYQ WHDQEWMARR KVLGETDQLH REPMSIYEVH
LPSWMRGQDG RYLSYRELAD RLVPHVKNMN FTHVEFLPLA HHPFEGSWGY QVTGLYAPYS
RLGNPDDFKY LVDTLHQANI GVFIDFVPAH FCKDSWGLVY YDGEPCYEYA DPREGEHKLW
GTAVFNYRRN EVRSFLLGAA YHWLRRYHID GLRIDAVSSM LYKNHQKKDG EWLPNEHGGD
ANLQAISLLQ ELNWVVHKEF PGVFTMAEES TSWRGVTDKA DGQATTQVHP TAPSVESSRR
LGFDAKWDLG WMNDTLSYLC CPVENRRKCH NKLTFRGLYM AHERWILPLS HDEVVSGKGS
LLDKCGYLGT PFEDRIRTLK TLYGFQIGMP GRPLIFMGGE IGQGREWKDN RSVDWHEGEE
ELRKKLCIWV SDLLGLYKSQ PALHAGDDET WNFKWTDCDN NNDCIVAFLR SYEFWFNDIL
VVCNFSPQAY YRYPVGVPHG GEWQLLLNSD DWKYAGGMCG RGNGSYIHTT QGGRLGWPYC
LWLDVPGNGC LYLKAPQPSA EEKRRMINES QRAKEPADRE GKTGDAGLKD QPEGSS
//
