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 25-MAY-2022, entry version 80.
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; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
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 EnsemblBacteria; ACL69450; ACL69450; Hore_06930.
DR KEGG; hor:Hore_06930; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_4_0_9; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
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; 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 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 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..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
