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Database: UniProt
Entry: GLGB_GLOVI
LinkDB: GLGB_GLOVI
Original site: GLGB_GLOVI 
ID   GLGB_GLOVI              Reviewed;         733 AA.
AC   Q7NL20;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {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 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=glr1306;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC89247.1; -; Genomic_DNA.
DR   RefSeq; NP_924252.1; NC_005125.1.
DR   RefSeq; WP_011141306.1; NC_005125.1.
DR   AlphaFoldDB; Q7NL20; -.
DR   SMR; Q7NL20; -.
DR   STRING; 251221.gene:10758787; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAC89247; BAC89247; BAC89247.
DR   KEGG; gvi:glr1306; -.
DR   PATRIC; fig|251221.4.peg.1331; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_3; -.
DR   InParanoid; Q7NL20; -.
DR   OrthoDB; 9800174at2; -.
DR   PhylomeDB; Q7NL20; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000557; 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:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR   CDD; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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   NCBIfam; TIGR01515; branching_enzym; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..733
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188709"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   733 AA;  84411 MW;  38B2FCBBF8C6EA00 CRC64;
     MNPTVELRDI EALVTNLHAD PFAILGPHRA EDGGAWVVRT YQPGASRVVL LGESGELAME
     NRRHPDLFEC AVPTAPGAYR LRVEDAWGER LIEDAYRFRG SLLSDLDGHL FAEGNHHRIY
     EKLGAHPAVF EGVAGVYFAV WAPSARNVSV LGDFNRWDGR FHQMRRVERS TGIWELFIPE
     LGEGTVYKFE IKNGFGHIYE KSDPYAFQQE LRPKSGSVVA DLDRYSWNDG EWLKRRALSN
     PLKQPLAIYE VHLGSWMRVP EEGDRFLSYT ELADKLIPYV KDLGFTHIEL LPILEHPFDG
     SWGYQVLGYY APTSRFGNPT EFMAFVDRCH QSGIGVILDW VPAHFPKDGH GLALFDGTHL
     YEHADSRQGE HKEWGTLVFN YGRNEVRNFL IANALFWFER YHIDGIRVDA VAAMLYLDYS
     RHDGEWVANR YGGRENLEAI GFLRQLNELI FLYYPGALSI AEESTAWPLV TRPPYLGGLG
     FNLKWHMGWM HDTLAYFRTD PLFRRYRHND ITFSITYTFY ENFVLALSHD EVVHMKGSII
     GKMPGDGWQK FANLRALFTF MYGHPGKKTL FMGMEFAHGR EWNAYQSLDW HLLDYPQHRQ
     MQQFVRALNR LYTGQPALYE EDCNPAGFFW VDCHDVLNSV FTFVRRGKDP SEQLLFVCNF
     TPTYHPHYRV GVLETGFWQE IFNSDSGIYG GSNKGNLGGL WSENWAIHGQ PYSLGLQLPP
     LGCLVFKRRK EQD
//
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