(data stored in ACNUC7421 zone)

SWISSPROT: GLGB_PARXL

ID   GLGB_PARXL              Reviewed;         736 AA.
AC   Q13S07;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685};
GN   OrderedLocusNames=Bxeno_B0164; ORFNames=Bxe_B2863;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic
CC       linkages in glycogen by scission of a 1,4-alpha-linked
CC       oligosaccharide from growing alpha-1,4-glucan chains and the
CC       subsequent attachment of the oligosaccharide to the alpha-1,6
CC       position. {ECO:0000255|HAMAP-Rule:MF_00685}.
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       {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
DR   EMBL; CP000271; ABE33132.1; -; Genomic_DNA.
DR   RefSeq; WP_011490512.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S07; -.
DR   SMR; Q13S07; -.
DR   STRING; 266265.Bxe_B2863; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABE33132; ABE33132; Bxe_B2863.
DR   GeneID; 4006772; -.
DR   KEGG; bxb:DR64_5192; -.
DR   KEGG; bxe:Bxe_B2863; -.
DR   PATRIC; fig|266265.5.peg.4828; -.
DR   eggNOG; ENOG4105C9C; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000283037; -.
DR   KO; K00700; -.
DR   OMA; EVVHGKS; -.
DR   OrthoDB; POG091H08D1; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001817; Chromosome 2.
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; -; 2.
DR   HAMAP; MF_00685; GlgB; 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; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13S07.
DR   SWISS-2DPAGE; Q13S07.
KW   Carbohydrate metabolism; Complete proteome; Glycogen biosynthesis;
KW   Glycogen metabolism; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    736       1,4-alpha-glucan branching enzyme GlgB.
FT                                /FTId=PRO_0000260641.
FT   ACT_SITE    415    415       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00685}.
FT   ACT_SITE    470    470       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00685}.
SQ   SEQUENCE   736 AA;  82135 MW;  4D7D9682B44E3CAC CRC64;
     MSEHDPAAGL QPLDIDALVE ARHPDPFSQL GLHHTDAGPV VRALLPNAAH VSVISRADGA
     LLGELEQLRP GLFAGRITSA APYRLRIDWH GVVQEIEDTY SFGPVLGDEP LGRLAGGDPY
     AVLECLGARP MEVDGVPGVR FAVWAPNARR VSVVGDFNAW DGRRHPMRLR HQAGVWELFV
     PRVGPGTRYK YELLSRDGHP LPLKADPCAM QTEKPPGTAS IVAHVDEVEQ FPWSDHEWIQ
     SRAGKQTARS PISIYEVHAE SWLRVAEEGQ RGLDWEELAE RMIPYVKSMG FTHVEFMPIA
     EHPFGGSWGY QPLGQFAPSA RFGKPEQFAR FVDKAHEAGL GVILDWVPAH FPNDAHGLID
     FDGTPLYEHA DPREGYHQDW NTMIYNLGRN EVSAFLIASG LAWLKRYHVD GLRVDAVASM
     LYRDYSRAAD QWVPNIYGGR ENLESIAFLK RLNHEVGYVP GVPGAITIAE ESTAWPGVTA
     RVEDGGLGFQ FKWNMGWMHD TLHYMEEDPV YRQYHHHNMT FGMVYAYSER FVLPLSHDEV
     VHGKGSLLGK MPGDRWQKFA NLRAYFGFMW THPGKKLLFM GGEFGQLAEF NHDASPHWHL
     LDDSNHHGVQ MLVRDLNRLY SDEPALYLLD CEPGGFEWLI GDDSGNSVFA YRRTDGAGRE
     LVVVCNMTPV PRLGYRIGMP RGGRWVEVLN TDAGVYGGSN MGNGGLIHTD SQSSHGWPHS
     AALTLPPLAT IVLRAD
//

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