GLGB1_XANAC
ID GLGB1_XANAC Reviewed; 724 AA.
AC Q8PR13;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 1;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 1;
DE AltName: Full=Glycogen branching enzyme 1;
DE Short=BE 1;
GN Name=glgB1; OrderedLocusNames=XAC0156;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE008923; AAM35048.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PR13; -.
DR SMR; Q8PR13; -.
DR STRING; 190486.XAC0156; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAM35048; AAM35048; XAC0156.
DR KEGG; xac:XAC0156; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000576; 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..724
FT /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT /id="PRO_0000188764"
FT ACT_SITE 403
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 456
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 724 AA; 80101 MW; A753B478470FC4C0 CRC64;
MSNRWDSGVV RALAEARHGD AFAVLGAHPS DKGRLLRTYL PGADRVGAVL DDGQVVALDA
GPEPGLFAGE LPAHGGYRLR IGWPGGEQET ADPYAFGPQL SDFDLHLISE GHHLQLADAL
GANVVEVEGV RGTRFAVWAP NASRVAVVGD FNSWDARRHP MRLRHQSGVW ELFVPDVGPG
AHYKYQLRGP HGHELPAKAD PVARRAELAP GTASIVADPT PHQWSDDGWM ATRARRQAHD
APMSIYEIHA GSWLREAGVD LDWDGLADRL IPYVADMGFT HVELMPVSEH PFGGSWGYQP
LGLFAPTARF GTPDGFARFV DRCHREGIGV IVDWVPAHFP TDAHGLAHFD GTALYEHADP
REGFHRDWNT LIYNHGRREV SGFLIASAME FLQRYHVDGL RVDAVASMLY RDYSRNAGEW
IPNIHGGREN YETIAFLRRL NEVVREHTPG AVMIAEESTA FPGVTAEVAH GGLGFHYKWN
MGWMHDTLHY AGLDPIYRRY HHGELTFSMV YAYSERFVLP ISHDEVVHGK GSLLGRMPGD
DWQRFANLRA YLGFMFTHPG RKLLFMGCEF GQPTEWNHDA GLPWHLLDDP RHRGVQTLVR
DLNRLYVQYP ALHAHDDDPS GFAWVVGDDA GNSVVAFLRK GKRGDAPVLV VINFTPVVQH
AYRIGVPQGG QWREVFNSDA GIYGGSNLGN GGSVTAEQQS MHGHAQSLPL LLPPLGAIVL
TPYG
