GLGB2_XANC5
ID GLGB2_XANC5 Reviewed; 743 AA.
AC Q3BYI0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB2 {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=XCV0452;
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}.
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DR EMBL; AM039952; CAJ22083.1; -; Genomic_DNA.
DR RefSeq; WP_011346122.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BYI0; -.
DR SMR; Q3BYI0; -.
DR STRING; 456327.BJD11_20610; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAJ22083; CAJ22083; XCV0452.
DR KEGG; xcv:XCV0452; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; IGGFWEL; -.
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..743
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000260717"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 475
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 743 AA; 81692 MW; 993B9A7E05F84474 CRC64;
MSERQGGQEQ RTEADGMTTE GISETSQTLQ ALANGLPADA FAVLGPKPLA EGRRQVRVLA
PGAEAMGLID PRGKLLARMQ ASAIDGVFEG ILAADGPYRL RIVWPDRVQE VEDPYAFAAT
LDESLLLQIA AGDGQAVRRA LGAQHVHCGD VPGVRFAVWA PHAQRVAVVG DFNGWDVRRH
PMRQRIGGFW ELFLPRVEAG ARYKYAVTAA DGRVLLKADP VARQTELPPA TASVVPSAAA
FAWTDAAWMA NRDPGAVPAP LSIYEVHAAS WRRDGHNQPL DWPTLAEQLI PYVQQLGFTH
IELLPITEHP FGGSWGYQPL GLYAPTARHG SPDGFAQFVD ACHRAGIGVI LDWVSAHFPD
DAHGLAQFDG AALYEHADPR EGMHRDWNTL IYNYGRPEVT AYLLGSALEW IEHYHLDGLR
VDAVASMLYR DYGRAEGEWV PNAHGGRENL EAVAFLRQLN REIATQFPGV LTIAEESTAW
PGVTAAISDG GLGFTHKWNM GWMHDTLGYM QRDPAERAQH HSQLTFGLVY AFDERFVLPL
SHDEVVHGTG GLLGQMPGDD WRRFANLRAY LALMWAHPGD KLLFMGAEFG QWADWNHDQS
LDWHLLDGAR HRGMQQLVGD LNAALRRTPA LYRGSHRADG FDWSVADDAR NSVLAFVRHD
PAGGAPLLAV SNLTPQPHHD YHVGVPRAGL WREILNTDSA HYGGSNLGNS GRLATEPVGM
HGHAQRLRLT LPPLATIYLQ AEK
