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Database: UniProt
Entry: A0A0J1GR52_9GAMM
LinkDB: A0A0J1GR52_9GAMM
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ID   A0A0J1GR52_9GAMM        Unreviewed;       717 AA.
AC   A0A0J1GR52;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ABT58_05355 {ECO:0000313|EMBL:KLV02151.1};
OS   Photobacterium aphoticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=754436 {ECO:0000313|EMBL:KLV02151.1, ECO:0000313|Proteomes:UP000036426};
RN   [1] {ECO:0000313|EMBL:KLV02151.1, ECO:0000313|Proteomes:UP000036426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25995 {ECO:0000313|EMBL:KLV02151.1,
RC   ECO:0000313|Proteomes:UP000036426};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) 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}.
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:KLV02151.1}.
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DR   EMBL; LDOV01000010; KLV02151.1; -; Genomic_DNA.
DR   RefSeq; WP_047873624.1; NZ_PYMF01000001.1.
DR   AlphaFoldDB; A0A0J1GR52; -.
DR   PATRIC; fig|754436.4.peg.1136; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000036426; 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; 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:UP000036426};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          237..622
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   717 AA;  81833 MW;  4CF1877485DD865E CRC64;
     MQLERAAFSD PFSFLGPQFQ SNGVALRVYM PGADSVAVLL ENGERIALSR EADSGFILEG
     EMDFTASLYQ LIVNWPHGEQ TFYDPYQFHD LIHSQSALVT PSQMYNEMGA QLITLNRNGK
     PVSGVRFLVF APHASAVSVI GHFNAWDGRR HSMQRLDDGL WGLFVPGLEE DTLYKYELKD
     STGNGLPHKA DPWGYHSEQY PSFASKVYNP ATYQWQDKAW QARPVTAKHQ EALSFYELHA
     GSWRTHPNGD MYNYRELADA LIPYLSEMGY THVELMPIAE HPFYGSWGYQ PIGLFAPSSR
     YGSPDDFKYF VDQCHKANIG VILDWVPAHF PSDDHGLANF DGTALFNDAD PRRGWHQDWQ
     SYIYDYGRDH VRRFLVANAL FWFEHYHIDG LRVDAVASML YLDYSREHDQ WIPNHEGGNV
     NFDAVSLLRW VNEEVYRHYP NAMTIAEEST AFPGVTKPTD MGGLGFGFKW NMGWMHDSLS
     YIKEESVHRK YHHNTITFPM VYAFSENYVL SLSHDEVVYG KGSLLNKMPG DEWQKTANLR
     AYMGYMYGQP GKKLNFMGAE IAQSAEWAHE GELEWHWLQY PRHSGMQALV KDLNHVYAAE
     PALYEQDCDP AGFEWRIQDD ADNSILAHER FALNGDKVLV VSNFTPVPRQ GYLLGVPAAG
     EYELLLNTDD SKYWGSQADV QSVMKTKKVA SHGLKQSISL DLPPLSTVFY RFTPAKK
//
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