GLGB_EMENI
ID GLGB_EMENI Reviewed; 684 AA.
AC Q9Y8H3; C8VN63; Q5BAW6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18;
DE AltName: Full=Glycogen-branching enzyme;
GN Name=be1; ORFNames=AN2314;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kobayashi T., Tanaka A., Matsuno A., Kato M., Tsukagoshi N.;
RT "Emericella nidulans putative branching enzyme.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA78714.1; Type=Miscellaneous discrepancy; Note=Probable sequencing error places a 'ESWIKTV' sequence at a wrong position.; Evidence={ECO:0000305};
CC Sequence=EAA64425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026630; BAA78714.1; ALT_SEQ; mRNA.
DR EMBL; AACD01000038; EAA64425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF86590.1; -; Genomic_DNA.
DR RefSeq; XP_659918.1; XM_654826.1.
DR AlphaFoldDB; Q9Y8H3; -.
DR SMR; Q9Y8H3; -.
DR STRING; 162425.CADANIAP00009008; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblFungi; CBF86590; CBF86590; ANIA_02314.
DR EnsemblFungi; EAA64425; EAA64425; AN2314.2.
DR GeneID; 2875628; -.
DR KEGG; ani:AN2314.2; -.
DR VEuPathDB; FungiDB:AN2314; -.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_2_1; -.
DR InParanoid; Q9Y8H3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 165238at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..684
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188782"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 395
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 34..40
FT /note="Missing (in Ref. 1; BAA78714)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="N -> NESWIKTV (in Ref. 1; BAA78714)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="K -> KVK (in Ref. 1; BAA78714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 78419 MW; D04B9091A92521BD CRC64;
MTSTAPSDGT GIIDLDPWLE PFREAIKRRF DYVESWIKTV DEVEGGLDKF SKGYEKFGFN
VSETGDITYR EWAPNAIEAA LVGDFNNWDT KANPMTRDNF GVWEIALPAK NGTPVIPHDS
KVKITMVTRS GERIYRIPAW IKRVVQDLNV SPIYESVFWN PPKAERYNFQ HARPKKPESL
RIYEAHVGIS SPDTRVATYK EFTANMLPRI KYLGYNAIQL MAIMEHAYYA SFGYQVNNFF
AASSRYGKPE DLKELVDTAH SMGLVVLLDV VHSHASKNVD DGLNMFDGSD HLYFHSGSKG
QHELWDSRLF NYGNHEVLRF LLSNLRFWME EYGFDGFRFD GVTSMLYTHH GIGTGFSGGY
HEYFGPAVDD DGVMYLALAN EMLHRLYPDC ITVAEDVSGM PALCLPHGLG GVGFDYRLAM
AIPDMYIKLL KEKSDNDWDI GNLAFTLTNR RHGEKTIAYA ESHDQALVGD KSLMMWLCDK
EMYTHMSVLT EFTPVIERGM ALHKMIRLVT HALGGEGYLN FEGNEFGHPE WLDFPRAGNN
NSFWYARRQL NLTEDHLLRY RFLNEFDRAM QLTESKYGWL HAPQAYISLK HEGDKVLVFE
RADLLWIFNF HPTESFTDYR VGVEQAGTYR VVLDTDDQAF GGLGRIDQGT RFFTTDMEWN
GRRNYLQVYI PTRTALALAL EETL
