GenomeNet

Database: UniProt
Entry: A0A2Z4GC17_9BACT
LinkDB: A0A2Z4GC17_9BACT
Original site: A0A2Z4GC17_9BACT 
ID   A0A2Z4GC17_9BACT        Unreviewed;       628 AA.
AC   A0A2Z4GC17;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN   ORFNames=DJ013_10680 {ECO:0000313|EMBL:AWV98608.1};
OS   Arcticibacterium luteifluviistationis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Arcticibacterium.
OX   NCBI_TaxID=1784714 {ECO:0000313|EMBL:AWV98608.1, ECO:0000313|Proteomes:UP000249873};
RN   [1] {ECO:0000313|EMBL:AWV98608.1, ECO:0000313|Proteomes:UP000249873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM1504 {ECO:0000313|EMBL:AWV98608.1,
RC   ECO:0000313|Proteomes:UP000249873};
RA   Li Y., Qin Q.-L.;
RT   "Complete genome sequence of Arcticibacterium luteifluviistationis SM1504T,
RT   a cytophagaceae bacterium isolated from Arctic surface seawater.";
RL   Submitted (MAY-2018) 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:0000256|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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC         Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC       Rule:MF_00685}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP029480; AWV98608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4GC17; -.
DR   KEGG; als:DJ013_10680; -.
DR   OrthoDB; 9761875at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000249873; 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   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; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000249873};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          152..503
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        364
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   628 AA;  72556 MW;  FB3005C8C6D109BA CRC64;
     MSFSLLSDYD IHLFKSGKHY KLYEKLGSHV VDNDGQKGTY FAVWAPNAEK VSVIGDFNGW
     NKTSHELNPR WDQSGIWETF IPEIGNGEVY KYFIKSNTGE ELEKADPFAL MWEKPPKTAS
     IVWDTYYEWS DKNWMDIRQD KNSLDSAYSV YEVHLGSWKR DPADNDRRLS YREIARDLVP
     YVKEMGFTHV ELMPIMHHPY EPSWGYQITG YFAASSIFGN PQDLMFLIEE LHKNEIGVIL
     DWVPSHFPGD ATGLFRFDGT ALYEHENPHE GYHPDWKSYI FNYGRFEVRS FLISNALFWL
     DRFHVDGLRV DAVASMLYRD YSRNEGEWIP NIHGGRENLE VISLLKEINE EVYASYPGTQ
     TIAEESTAFP GVSRPTFSGG LGFGMKWMMG WMNDTLAYFE KDAAFRKFHQ KDITFSTVYA
     FTENFMLPLS HDEVVYGKGS LLDKMPGDDW QKFANLRLLY TYMFTHPGAK LLFMGGEFGQ
     KAEWDFKNSL DWHELENPLN KGMAELVKGL NNIYKTEESL TLNQFSHTAF QWIDTMDEEN
     SILFYKRQTE TEEVYIVLNM TPVPRDSYQL GVDKAGTYQE LLNSDDGHFG GSGISNGSFK
     AKKAPYHGLD YSVIIDLPPL AGVIFKRK
//
DBGET integrated database retrieval system