GLGB_BACSU
ID GLGB_BACSU Reviewed; 627 AA.
AC P39118;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Glycogen branching enzyme;
DE Short=BE;
GN Name=glgB; OrderedLocusNames=BSU30980;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8145641; DOI=10.1111/j.1365-2958.1994.tb00301.x;
RA Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT "Glycogen in Bacillus subtilis: molecular characterization of an operon
RT encoding enzymes involved in glycogen biosynthesis and degradation.";
RL Mol. Microbiol. 11:203-218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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.
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 -!- INDUCTION: Expressed exclusively on media containing carbon sources
CC that allow efficient sporulation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; Z25795; CAA81040.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00214.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15076.1; -; Genomic_DNA.
DR PIR; S40048; S40048.
DR RefSeq; NP_390976.1; NC_000964.3.
DR RefSeq; WP_004398803.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39118; -.
DR SMR; P39118; -.
DR STRING; 224308.BSU30980; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P39118; -.
DR PRIDE; P39118; -.
DR EnsemblBacteria; CAB15076; CAB15076; BSU_30980.
DR GeneID; 937993; -.
DR KEGG; bsu:BSU30980; -.
DR PATRIC; fig|224308.179.peg.3357; -.
DR eggNOG; COG0296; Bacteria.
DR InParanoid; P39118; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; P39118; -.
DR BioCyc; BSUB:BSU30980-MON; -.
DR BRENDA; 2.4.1.18; 658.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001570; 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; -; 1.
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; 2.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..627
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188683"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 73665 MW; 64B0A5553B6767BA CRC64;
MAAASPTAHD VYLFHEGSLF KSYQLFGSHY RELNGKSGYE FCVWAPHASE VRVAGDFNSW
SGEEHVMHRV NDNGIWTLFI PGIGEKERYK YEIVTNNGEI RLKADPYAIY SEVRPNTASL
TYDLEGYSWQ DQKWQKKQKA KTLYEKPVFI YELHLGSWKK HSDGRHYSYK ELSQTLIPYI
KKHGFTHIEL LPVYEHPYDR SWGYQGTGYY SPTSRFGPPH DLMKFVDECH QQNIGVILDW
VPGHFCKDAH GLYMFDGEPL YEYKEERDRE NWLWGTANFD LGKPEVHSFL ISNALYWAEF
YHIDGFRVDA VANILYWPNQ DERHTNPYAV DFLKKLNQTM REAYPHVMMI AEDSTEWPQV
TGAVEEGGLG FHYKWNMGWM NDVLKYMETP PEERRHCHQL ISFSLLYAFS EHFVLPFSHD
EVVYGKKSLL NKMPGDYWQK FAQYRLLLGY MTVHPGKKLI FMGSEFAQFD EWKDTEQLDW
FLDSFPMHQK ASVFTQDLLR FYQKSKILYE HDHRAQSFEW IDVHNDEQSI FSFIRYGQKH
GEALVIICNF TPVVYHQYDV GVPFFTQYIE VLNSDSETYG GSGQINKKPL SAKKGALHHK
PCYITMTIPP YGISILRAVK KRGEIKR
