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Database: UniProt
Entry: A0A1I2PDJ4_9FIRM
LinkDB: A0A1I2PDJ4_9FIRM
Original site: A0A1I2PDJ4_9FIRM 
ID   A0A1I2PDJ4_9FIRM        Unreviewed;       847 AA.
AC   A0A1I2PDJ4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05216356_10275 {ECO:0000313|EMBL:SFG13610.1};
OS   Oribacterium sp. WCC10.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=1855343 {ECO:0000313|EMBL:SFG13610.1, ECO:0000313|Proteomes:UP000199160};
RN   [1] {ECO:0000313|EMBL:SFG13610.1, ECO:0000313|Proteomes:UP000199160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCC10 {ECO:0000313|EMBL:SFG13610.1,
RC   ECO:0000313|Proteomes:UP000199160};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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.
CC       {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-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}.
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DR   EMBL; FOPH01000002; SFG13610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2PDJ4; -.
DR   STRING; 1855343.SAMN05216356_10275; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000199160; 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; 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; 2.
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          261..619
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          757..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        482
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   847 AA;  96937 MW;  AF211DE761F68C7F CRC64;
     MTEKLYDVMN WADVEDVTYA ETADPKSILG AHVIPEGLLI QAFIPTAKDI EVKIQGDRVY
     QMELADEEGF FAVLVPMKKK WEKELPKFSY LITYDNDTTM ESEDPYSFAS IYTEEDIKKY
     QAGIWYDIYN KMGAHPITID GVEGVVFSVW APNAERVSVV GDFNLWDGRR NMMQCLGASG
     IFEIFIPHLT PGTIYKYEIK CRHKEPFLKT DPYANAMEMR PNNASVVAEL DKFEWTDKEW
     EDRKLELKTS GIKELPMSVY EVHLGSFARK QSMINEDGTE VAGSEFYNYK ELAKKLAAYV
     KKQGYTHVEL MPIMEHPLDA SWGYQVSGYY APTSRYGSPE DFMYFVNYMH NEGIGVILDW
     VPAHFPRDAW GIAQFDGTGL YENPDPLLAS HPHWGTLTFN YRKNEVSNFL IGSAMYWADK
     YHVDGLRMDA VASMLYLDYG RQGQSVSRNM YGGNENLDSV EFLKHLNSQF HKRFPGTLLI
     AEESTAWPNI TGSVKDDGLG FDIKWNMGWM NDFLGYMETD PYFRKGSYNQ LTFSMIYNYS
     EDFMLVFSHD EVVHGKRSLL GKMPGHTFEE KSRNLRTAYG YFWSHPGKKL LFMGQDFGQY
     DEWSENQELE WNLLEYPVHK ELQSFVKDLN DVYRSQPALW QLDYYPDGFE WINCSYSDLS
     MVMFVRKTDK PEDTVLVVTN FDNVAHPKFR VGVPFMCNAK ALISTDDEKY GGFGMVKRTQ
     IKAKKISWDD RDYALDIDIP SMSTTIYKLT PCEEPEIKES SKSTATKKTA RKPAAKKTSS
     KKDEKEEVIE VSAVEKVSVG KTTAKATKTT TAKTVKKVQT ESGKSTLKPA AAKAPKKASG
     AARRRKG
//
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