ID A0A0V0QYB4_PSEPJ Unreviewed; 753 AA.
AC A0A0V0QYB4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PPERSA_08717 {ECO:0000313|EMBL:KRX07040.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX07040.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX07040.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX07040.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX07040.1}.
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DR EMBL; LDAU01000089; KRX07040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QYB4; -.
DR EnsemblProtists; KRX07040; KRX07040; PPERSA_08717.
DR InParanoid; A0A0V0QYB4; -.
DR OMA; YEMHLGS; -.
DR OrthoDB; 96at2759; -.
DR Proteomes; UP000054937; 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:UP000054937};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 249..600
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 753 AA; 88296 MW; 1BD3CEA506A6770A CRC64;
MKPSYLDGED QISQKFQTQQ KCRPKRRSVF YQQAPSLQET DHMHNSSDLH SSQGHKEEKL
PDKDFKCVSE LQVFKDDPYL HDHVDHFQYR NKQYNLTLDR IEAAEGNLIN FANSYKQRGF
YEDDEENIVY QEWAPGAKEM YLTGEFCSWD RKQHKMQKGE YGTWKIVLPK GTIPHDTKVK
VHLLDANNNW VDRIPVYINY AVQFENKHFD GVYWNPQEKY QFIHPKPSKA RAPKIYECHI
GMSGIEPKVH SFNYFRENVL PRIAKLGYNC IQIMAIAEHP YYGSFGYHVS LPFAISSRFG
TPEDFKKLVD QAHFYGIQVL IDIVHSHIAK NVDDGINQWD GTDHMYFHSG EKGQNKLWDS
RLYNYNNYET LRLLISNLQY FLVEYNVDGF RFDGVTSMLY HHHGIGVGFT GGYHEYFGMQ
FDVESAVYLM LANKLIHTTN PEAISIAEDV SGYPTLCRSH RDGGMGFDFR LQMAVPDKWI
KLLKEVKDED WNIGDIVHTL TNRRYKEPCI TYAESHDQAL VGDKTLSMWL FDKEIYDNMS
KMSHETLVIS RGMALHKMLR LITLVMGGEG YLNFMGNEFG HPEWIDFPRD GNNWSYQHCR
RRWDICDDKN LRYNQLFEFE AAMQYVENFF QFLDKPQNFV NEKHESNKVI VYEKSNLLFV
FNFHPNKSYE NYKVGTHLEG DHIIVLDTDS KKFGGYGRLD AGHTQAFPYH KDGQNGRPFS
INLYIPARTA QVLCLVKDKE NMQYKDNTLN LED
//
