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Database: UniProt
Entry: A0A2T0U9K2_9SPHI
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Original site: A0A2T0U9K2_9SPHI 
ID   A0A2T0U9K2_9SPHI        Unreviewed;       646 AA.
AC   A0A2T0U9K2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=B0I27_102369 {ECO:0000313|EMBL:PRY54600.1};
OS   Arcticibacter pallidicorallinus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1259464 {ECO:0000313|EMBL:PRY54600.1, ECO:0000313|Proteomes:UP000238034};
RN   [1] {ECO:0000313|EMBL:PRY54600.1, ECO:0000313|Proteomes:UP000238034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9313 {ECO:0000313|EMBL:PRY54600.1,
RC   ECO:0000313|Proteomes:UP000238034};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRY54600.1}.
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DR   EMBL; PVTH01000002; PRY54600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0U9K2; -.
DR   OrthoDB; 9761875at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000238034; Unassembled WGS sequence.
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:UP000238034};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          161..511
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        372
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   646 AA;  74732 MW;  41BE49EC0D60D38D CRC64;
     MNMSGNLANQ EFSLFTDFDI ALFKAGKHYH LYNKLGAHRV NHQGRWGAYF AVWAPNARYV
     SVVGNFNSWN SGDHPMQVRW DESGIWEVFI PDVGHAEYFK YYIEGPNGYS VEKGDPYAFH
     WETPPQTASV VWDCKYSWND TEWMQSRQRE NPLKKPISVY ELHIGSWRKN GEDGSFLTYR
     EIAGQLPEYC VYMGFTHVEF MPVMEHPFFG SWGYQLTGYF APSSRFGTPE DFMYLVDQLH
     LAGIGVILDW VPSHFPVDEH GLGYFDGTPL YEYADPRKGF HPDWKSNIFN LERNEVREFL
     ISNAFYWLDK FHIDGLRVDA VASMLYLDYS RNEGEWIPNI YGGRENLEAI SFLQEFNEAV
     HSFFPDVLTI AEESTSWPGV TQPVQQGGLG FDMKWMMGWM HDSLNYFQKE PVYRRYHHGQ
     LTFSLVYAFS EKFCLPLSHD EVVHGKASLI NKMPGDAWQK AANLRLLYAY MYGHPGAKLI
     FMGGEFAQAH EWQHDYSLDW HENHQPLNRG IQLLLKDLNE LYKTPAMHQL DFSSDGFCWI
     DCCDADRSIL SWIRKGERAG DELLFVANFT PEVRHNYRLG VHVPGFYEEI LNSDNLKYGG
     SDVLNEGELE AFPVSVSGFT HSLSISVPPL GISVLKFSRE NPDYIF
//
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