GLGB1_STRCO
ID GLGB1_STRCO Reviewed; 774 AA.
AC Q59833; Q9L1K4;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 25-MAY-2022, entry version 142.
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; Synonyms=glgBI; OrderedLocusNames=SCO5440; ORFNames=SC6A11.16c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8596463; DOI=10.1111/j.1365-2958.1995.mmi_18010089.x;
RA Bruton C.J., Plaskitt K.A., Chater K.F.;
RT "Tissue-specific glycogen branching isoenzymes in a multicellular
RT prokaryote, Streptomyces coelicolor A3(2).";
RL Mol. Microbiol. 18:89-99(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RC STRAIN=A3(2) / NRRL B-16638;
RA Schneider D., Bruton C.J., Chater K.F.;
RT "Duplicated gene clusters reveal a possible 'carbon relay' during aerial
RT mycelium development in Streptomyces coelicolor A3(2).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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; X83397; CAA58314.1; -; Genomic_DNA.
DR EMBL; AL939123; CAB72416.1; -; Genomic_DNA.
DR EMBL; AJ001205; CAA04603.1; -; Genomic_DNA.
DR PIR; S70079; S70079.
DR RefSeq; NP_629578.1; NC_003888.3.
DR RefSeq; WP_011030247.1; NC_003888.3.
DR AlphaFoldDB; Q59833; -.
DR SMR; Q59833; -.
DR STRING; 100226.SCO5440; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 1100880; -.
DR KEGG; sco:SCO5440; -.
DR PATRIC; fig|100226.15.peg.5521; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR InParanoid; Q59833; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; Q59833; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..774
FT /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT /id="PRO_0000188749"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 510
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 146
FT /note="T -> R (in Ref. 1; CAA58314/CAA04603)"
FT /evidence="ECO:0000305"
FT CONFLICT 766..774
FT /note="GTAARRASG -> WHGRPASIRLTLPPLATVWLRPA (in Ref. 1;
FT CAA58314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 85451 MW; 1D55555330F249BF CRC64;
MTPRPSSSGP DPRKTTGKKP AGKTPTGKKP AKAAKKKAPR RTTASANASA TTSVSGAEVA
VSPAPDAADR ERLLAGTHHD PHAVLGAHRV PGGVAFRVFR PYALAVTVLS GELRVGLHDD
GDGFFSGLVP LKDVPAHRLL VAYEGTEQEV EDPYRFLPTL GELDLHLLGE GRHEQLWRAL
GAHPTTHEGV AGTRFAVWAP NARGVRVAGG FNFWDGTGHP MRSLGSTGVW ELFLPGVGAG
ELYKFEITRP DGSRTFRADP LARRTEVPPA TSSVVHASDY TWGDEEWLAH RADAPAHEAP
MSVYEVHLPS WRPGLTYRQL AEQLPAYVAD LGFTHVELMP VAEHPFGGSW GYQVTGFYAP
TARLGDPDDF KYLVDRLHRA GIGVLMDWVP AHFPRDDWAL AEFDGRPLYE HSDPLRAAHP
DWGTLEFDFG RREVRNFLVA NAVYWCEEFH IDGLRVDAVA SMLYLDYSRE PGEWEPNEHG
GRENLDAVAF LQEMNATLYR RVPGVVTVAE ESTAWDGVTR ATHHEGPSGF GGLGFGLKWN
MGWMHDSLDY MSHEPVHRKH HHGEMTFSMV YAYSENYVLP ISHDEVVHGK RSLVSKMPGD
WWQQRANERA YLGFMWAHPG KQLLFMGQEF AQGAEWSEAH GPDWWLLDPE YGASADHRGV
RDLVRDLNTV YRATPALWRR DTHPSGFSWV VGDAAEDNVL AFLRLDADGT PLLAVSNFAP
VVRSGYRLGV PDEVPAWHEV LNTDAARYGG GDVVNPDPVK PEPQGGTAAR RASG
