ID A6R9G2_AJECN Unreviewed; 701 AA.
AC A6R9G2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=HCAG_06953 {ECO:0000313|EMBL:EDN09786.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN09786.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476660; EDN09786.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R9G2; -.
DR STRING; 339724.A6R9G2; -.
DR VEuPathDB; FungiDB:HCAG_06953; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR OMA; YEMHLGS; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000009297; 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:UP000009297};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 207..567
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 409
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 701 AA; 79710 MW; 8844203D8AA243FA CRC64;
MAAGQGLDDV VAAAVARETT PDGSGVVKLD PWLEPFKDAL RSRFSHTNQW IQTINETEGG
LEVFSRGYEK FGFNVRDNGD IVYREWAPNV VDAHLIGDFN NWDRKATPMQ RNDFGVWEVT
VLAKDGIPII PHNSKVKITM TAPSGEQLDR FPAWIKRVTQ NLSVSPEFHA IFWNPPAQDR
YAFKQPHPPK PASLRIYEAH VGISSPETRV ATYKEFTKNM LPRIHGLGYN AIQLMAIMEH
AYYASFGYQV NNFFAASSRY GTPEELKELI DTAHGLGLVV LLDVVHSHAS KNVLDGLNMF
DGTDNLYFHA GPKGQHELWD SRLFNYGNHE VLRFLLSNLR FWMEEYQFDG FRFDGVTSML
YMHHGIGTGF SGGYHEYFGP SVDEDGITYL MLANEMLHQI YPNCITVAED VSGMPALCLP
LTLGGQGFDY RLAMAIPDMY IRLLKEQKDE EWNMGHLTFT LTNRRYGEKT IAYAESHDQA
LVGDKSLMMW LCDKELYTHM SVLTELTPVI ARGLSLHKMI RLLTHGLGGE GYLSFEGNEF
GHPEWLDFPR AGNNNSYWYA RRQLNLTEDP LLRYKFLNDF DRAMQVAEEK YGWLHAPQAF
VSQKHEENKV IVFERAGLVW VFNFHATRSW ADYMIGVGGK GRTYRIVLDT DAEGFGGFGR
VEAGTRFFTR GEGWDGREDS LMVYVPTRTA LVLAPEEETE G
//
