GLGB1_XANC5
ID GLGB1_XANC5 Reviewed; 732 AA.
AC Q3BZE1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 1 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB1 {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=XCV0141;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC growing alpha-1,4-glucan chains and the subsequent attachment of the
CC oligosaccharide to the alpha-1,6 position. {ECO:0000255|HAMAP-
CC Rule:MF_00685}.
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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM039952; CAJ21772.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BZE1; -.
DR SMR; Q3BZE1; -.
DR STRING; 456327.BJD11_22230; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAJ21772; CAJ21772; XCV0141.
DR KEGG; xcv:XCV0141; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000007069; Chromosome.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
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.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..732
FT /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT /id="PRO_0000260716"
FT ACT_SITE 411
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 464
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 732 AA; 80866 MW; 1B058133E21604B0 CRC64;
MMSGVMTAVS NRWDPGAVRA LAEARHGDAF AVLGAHPSDN GRFLRTYLPG ADRVSAVLDD
GQVVALDAGP EPGLFAGELP AHGGYRLRIG WPGGEQETAD PYAFGPQLSD FDLHLISEGH
HLQLADALGA NVVEVDGVRG TRFAVWAPNA SRVAVVGDFN SWDARRHPMR LRHQAGVWEL
FVPDVGPGAH YKYQLRGPHG HELPAKADPV ARRAELAPGT ASIVADPTPH QWSDDGWMAT
RARRQAHDAP MSIYEIHAGS WLREAGLDLD WDGLADRLIP YVADMGFTHV ELMPVSEHPF
GGSWGYQPLG LFAPTARFGT PDGFARFVDR CHREGIGVIV DWVPAHFPTD AHGLAHFDGT
ALYEHADPRE GFHRDWNTLI YNHGRREVSG FLIASAMEFL QRYHVDGLRV DAVASMLYRD
YSRNAGEWIP NIHGGRENYE TIAFLRRLNE VVREHTPGAV MIAEESTAFP GVTADVAHGG
LGFHYKWNMG WMHDTLHYAG LDPIYRRYHH GELTFSMVYA YSERFVLPIS HDEVVHGKGS
LLGRMPGDDW QRFANLRAYL GFMFTHPGRK LLFMGCEFGQ PTEWNHDAGL PWHLLDDPRH
RGVQTLVRDL NRLYVQYPAL HAHDDDPSGF AWVVGDDAGN SVVAFLRKGK RGDAPVLVVI
NFTPVVQHGY RIGVPQGGQW REVFNSDAGI YGGSNLGNGG SVTAEQQSMH GHAQSLPLLL
PPLGAIVLTP YG
