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Database: UniProt
Entry: GLGB_HALOH
LinkDB: GLGB_HALOH
Original site: GLGB_HALOH 
ID   GLGB_HALOH              Reviewed;         630 AA.
AC   B8CVY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=Hore_06930;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69450.1; -; Genomic_DNA.
DR   RefSeq; WP_012635638.1; NC_011899.1.
DR   AlphaFoldDB; B8CVY1; -.
DR   SMR; B8CVY1; -.
DR   STRING; 373903.Hore_06930; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; hor:Hore_06930; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_4_0_9; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000719; 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; 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; 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   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; 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..630
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_1000147759"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   630 AA;  74401 MW;  C07E9BEBE09C7775 CRC64;
     MKDKIPTDYD RYLFHQGSHY KSYEFLGAHP CEENGKTGVR FSVWAPNAAE VRVIGSFNNW
     DGNINPMERI NDSGIWTTFI PEAKKGDLYK YEILTKYGDT RIKSDPYAFY AERKPKTASI
     VYSLNNYKWN DKKWMDKKKD YTVYNKPVLI YEVHLGSWKR KENGDYLTYR ELANELVEYV
     KDMGYNYIEL LPVAEHPFDG SWGYQLTNYY SVTSRYGTPE DFMYFIDKCH QNGIGVILDW
     VPGHFCKDDH GLRLFDGTAL YEPQDPRKAE NEWDTLNFDF NQPEVWSFLI SNAVFWFDIY
     HIDGLRVDAV SNLLYLNHGK GDGEWVPNKY GGHENLEAID FIKTLNKVIF EYFPNPLMIA
     EESSAWPLVT YPAHLGGLGF NYKWNMGWMN DTLEYMEMDS IYRKYHHNLL TFSFMYMFSE
     NFVLPLSHDE VVHGKKSLLD KMPGDYWQKF ANLRTLYGYM MGHPGKKLLF MGGEFGQFIE
     WNYKQGLDWL LLDYDMHKKL QNYVRELNYF YRQEKTLWEG DHEDGGFEWI DPHDSEQSII
     TFMRKNKDGS DYTIIVCNFT PEVRHNYRIG VPEFKEYKEV FNSDLEKFGG SGQKNSTIIQ
     PSEQPWHNRP YSIEITIPPL ATIFFKPLNQ
//
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