ID A0A0A2J9J0_PENEN Unreviewed; 689 AA.
AC A0A0A2J9J0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=1,4-alpha-glucan-branching enzyme {ECO:0000256|ARBA:ARBA00020932};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE AltName: Full=Glycogen-branching enzyme {ECO:0000256|ARBA:ARBA00031979};
GN ORFNames=PEX2_107410 {ECO:0000313|EMBL:KGO52082.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO52082.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO52082.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO52082.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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 -!- 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}.
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:KGO52082.1}.
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DR EMBL; JQFZ01000274; KGO52082.1; -; Genomic_DNA.
DR RefSeq; XP_016594851.1; XM_016748009.1.
DR AlphaFoldDB; A0A0A2J9J0; -.
DR STRING; 27334.A0A0A2J9J0; -.
DR GeneID; 27683430; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR OrthoDB; 96at2759; -.
DR PhylomeDB; A0A0A2J9J0; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000030143; 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:UniProtKB-UniPathway.
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:UP000030143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 198..514
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 400
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 689 AA; 78688 MW; 7C8685E134D4D567 CRC64;
MSSTIDSSNI PTDGTGVIQL DPWLEPHRDV LKHRYQVVED WAKAINETEG GLDKFSKGYE
TFGLHVQPNG EIKYQEWAPN AQEASLVGEF NNWDVNANPM TKNSFGIWNV TVPAKNGAAA
IPHDSKIKIS MVLPSGERIY RLPAWIKRVV QDLNVSPAYD AVFWNPPAED LYKFQHARPK
KPESLRIYEA HVGISSPETR VATYKEFTKN MLPRIKYLGY NAIQLMAIME HAYYASFGYQ
VNNFFAASSR YGSPEDLKEL VDTAHSMGLV VLLDVVHSHA SKNVIDGLNE FDGTDHLYFH
GGAKGRHELW DSRLFNYGSH EVLRFLLSNL RFWMEEYKFD GYRFDGVTSM LYTHHGIGTG
FSGGYHEYFG PSVDEEGVTY LTLANEMLHE LYPECITVAE DVSGMPALCL PHKLGGAGFD
YRLAMAVPDM WIKLLKESTD DEWDMANISF TLTNRRHGEK TIAYAESHDQ ALVGDKTLMM
WLCDKEMYTH MSTLTEFTPV IERGMALHKM IRLVTHALGG EGYLNFEGNE FGHPEWLDFP
REGNDNSFWY ARRQLNLTED PLLRYHFLNE FDRGMQLAEQ KYGWLSSSQA YISLKNESDK
VLVFERAGLL WIFNFNSKKS FTDYRVGVDV PGTYRIVLDT DEKEFGGLGR NVKETRFFTT
DMGWNGRGNF VQVYIPTRTA LVLALEETL
//
