GLGB_CANGA
ID GLGB_CANGA Reviewed; 706 AA.
AC Q6FJV0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18;
DE AltName: Full=Glycogen-branching enzyme;
GN Name=GLC3; OrderedLocusNames=CAGL0M03377g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR380959; CAG62470.1; -; Genomic_DNA.
DR RefSeq; XP_449494.1; XM_449494.1.
DR AlphaFoldDB; Q6FJV0; -.
DR SMR; Q6FJV0; -.
DR STRING; 5478.XP_449494.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblFungi; CAG62470; CAG62470; CAGL0M03377g.
DR GeneID; 2891502; -.
DR KEGG; cgr:CAGL0M03377g; -.
DR CGD; CAL0136349; CAGL0M03377g.
DR VEuPathDB; FungiDB:CAGL0M03377g; -.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_2_1; -.
DR InParanoid; Q6FJV0; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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 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 3: Inferred from homology;
KW Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..706
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188779"
FT ACT_SITE 358
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 419
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 81044 MW; 18872CAADBCD2A87 CRC64;
MSLTKIPENV QGAVSIDPWL EPFADVLSER RYLADKWLYD IKHATPDGSE QSLVDFARNA
YKTYGLHANQ QTKEIVYREW APNAQRAFLV GEFNNWNEES HEMKHKDEFG VFSITLAPLE
NGDFAIPHDS KIKVMFVLPD GSKVYRIPAW ITRATQPSKE TAQKYGPTYE GRFWNPPNSY
QFKHQRPKFN LANDSIKIYE AHIGISSPEP KVASYKEFTQ NVLPRIKHLG YDAIQLMAIM
EHAYYASFGY QVTNFFAISS RYGTPEDLKE LIDTAHSMGI LVLLDVIHSH ASKNSEDGLN
MFDGSDHQYF HSLTSGRGEH PLWDSRLFNY GSFEVQRFLL ANLAYYIDVY QFDGFRFDGV
TSMLYLHHGV GAGGAFSGDY NEYLSRDRSG VDHEALAYLM LANDLVHDLL PESAVTIAED
VSGYPTLCLP RTAGGGGFDY RLAMALPDMW IKLLKTKQDD DWDMGHIVHT LTNRRHGEKV
VAYCESHDQA LVGDKTLAFW LMDAAMYTDM TVLKEPTLVI DRGIALHKMI RLITHSLGGE
AYLNFEGNEF GHPEWLDFPR VGNNDSYHYA RRQFNLVDDD LLRYRHLNEF DAAMQNCESK
HQWLNTPQAY VSLKHEVDKV IAFERNGHLF VFNFHPTQSF TDYRIGVDVA GTYKIVLNTD
RAEFGGHNRI DEAQEFFTTD LEWNNRRNFI QVYIPSRTAI VLTRQM