(data stored in ACNUC8465 zone)

SWISSPROT: 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   30-AUG-2017, entry version 91.
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 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       chain to a primary hydroxy group in a similar glucan chain.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR380959; CAG62470.1; -; Genomic_DNA.
DR   RefSeq; XP_449494.1; XM_449494.1.
DR   ProteinModelPortal; Q6FJV0; -.
DR   SMR; Q6FJV0; -.
DR   STRING; 284593.XP_449494.1; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblFungi; CAG62470; CAG62470; CAGL0M03377g.
DR   KEGG; cgr:CAGL0M03377g; -.
DR   CGD; CAL0136349; CAGL0M03377g.
DR   EuPathDB; FungiDB:CAGL0M03377g; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000175159; -.
DR   InParanoid; Q6FJV0; -.
DR   KO; K00700; -.
DR   OMA; EVVHGKS; -.
DR   OrthoDB; EOG092C0QFK; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; 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   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR006407; GlgB.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
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; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJV0.
DR   SWISS-2DPAGE; Q6FJV0.
KW   Complete proteome; Glycogen biosynthesis; Glycosyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    706       1,4-alpha-glucan-branching enzyme.
FT                                /FTId=PRO_0000188779.
FT   ACT_SITE    358    358       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    419    419       Proton donor. {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
//

If you have problems or comments...

PBIL Back to PBIL home page