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Database: UniProt
Entry: A0A0C5WFX7_9GAMM
LinkDB: A0A0C5WFX7_9GAMM
Original site: A0A0C5WFX7_9GAMM 
ID   A0A0C5WFX7_9GAMM        Unreviewed;       713 AA.
AC   A0A0C5WFX7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=H744_1c1023 {ECO:0000313|EMBL:AJR06048.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06048.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR06048.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR06048.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) 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; CP005973; AJR06048.1; -; Genomic_DNA.
DR   RefSeq; WP_044621236.1; NZ_CP005973.1.
DR   AlphaFoldDB; A0A0C5WFX7; -.
DR   STRING; 658445.H744_1c1023; -.
DR   KEGG; pgb:H744_1c1023; -.
DR   PATRIC; fig|658445.3.peg.1104; -.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000032303; Chromosome 1.
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; 2.
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:UP000032303};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          237..576
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        394
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        447
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   713 AA;  81252 MW;  1C8D5B5B3E3367C4 CRC64;
     MQLERAAFSD PFSFLGPQYQ SNDIALRVYM PGADSIEAIT ENGERFTLAR EADSGFVLGG
     DFDFTTALYQ LVVNWPQGEQ TIYDPYQFHN LIQSGEALAD PSLMHSEMGA QLVTLNRGNS
     SISGVRFLVF APNASAVSVV GHFNAWDGRR HPMQRLDDGL WGLFIPELEE GTHYKFELKD
     SAGEGLPHKA DPWGYESEQY PSFASKVYDQ AKYTWQDGAW QNRPVTAKHQ QALSFYELHA
     GSWRKNDQGE FLNYRELADE LIPYLSDMGY THVELMPVSE HPFYGSWGYQ PIGLFAPTSR
     FGSPDDFKYF VDQCHQANIG VVLDWVPAHF PSDEHGLANF DGTALFNDPD PRRGWHQDWQ
     SYIYDYGRDH VRRFLVSNAL FWFEHYHIDG LRVDAVASML YLDYSREHDQ WIPNHEGGNV
     NFDAVSLLRW VNEEVYRHYP NAMTIAEEST AFPGVTKPTD MGGLGFGFKW NMGWMHDSLS
     YIKEEPIHRS YHHNTITFPM VYAFSENYVL SLSHDEVVYG KGSMLDKMPG DEWQKTANLR
     AYMGYMYGQP GKKLNFMGAE IAQSAEWNHD GQLEWHWLQY PRHSGMQALV KDLNALYTSE
     PAMYEQDCDP AGFEWRVQDD AGNSILAHER IALNGDKVLV VSNFTPVPRE GYLLGVPAEG
     EYELLLNTDD EKYWGSNAPV KASIATEQVA SHGLEQSIAV DLPPLATVFY RFK
//
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