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Database: UniProt
Entry: A0A1U7D9L1_9RHOB
LinkDB: A0A1U7D9L1_9RHOB
Original site: A0A1U7D9L1_9RHOB 
ID   A0A1U7D9L1_9RHOB        Unreviewed;       727 AA.
AC   A0A1U7D9L1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=Ga0080559_TMP3996 {ECO:0000313|EMBL:APX24792.1};
OS   Salipiger profundus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX24792.1, ECO:0000313|Proteomes:UP000186559};
RN   [1] {ECO:0000313|EMBL:APX24792.1, ECO:0000313|Proteomes:UP000186559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2016 {ECO:0000313|EMBL:APX24792.1,
RC   ECO:0000313|Proteomes:UP000186559};
RA   Tang K.;
RT   "Deep-sea bacteria in the southern Pacific.";
RL   Submitted (MAR-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; CP014796; APX24792.1; -; Genomic_DNA.
DR   RefSeq; WP_076624555.1; NZ_CP014796.1.
DR   AlphaFoldDB; A0A1U7D9L1; -.
DR   STRING; 1229727.Ga0080559_TMP3996; -.
DR   KEGG; tpro:Ga0080559_TMP3996; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000186559; 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; 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:UP000186559};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          249..603
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        459
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   727 AA;  81847 MW;  084F58C4D47BD08A CRC64;
     MTDAKHPTAS DFQRLIQGHH DDPFALLGPH FADDTQYVTA FDPGAHQMWA VIDGTSHPLD
     PVQDAPGVFR GKVPGDAPYH LKGAAQGSEW EFEDAYRFGP VLGEVDEYLL GEGRHHRMWE
     ALGAHIREHE GCWGTQFAVW APNAQRVSVV GEFNWWNGLR HSMRRRGATG VWEIFIPNVT
     DGAIYRYEIV GPDGTIQPLK ADPVGFGSEH PPANASIVRD ITGYGWSDDA WMTTRAEAQK
     REAPISVYEV HLPSWRRKND NRPISYIEAA QELVEYVTEM GFTHIELLPI SEYPFDGSWG
     YQPVGLFAPT IRCGLPHEFR DLVNAAHRAG LGIILDWVPG HFPTDPHGLG KFDGTALYEH
     ADPREGFHRD WNTLIYNYGR AEVANFLTAN ALYWLEEYHA DGLRVDAVAS MLYRDYSRNP
     GEWVPNKDGG RENYEAIDLL RRVNTESYGE NPGIMTVAEE STAYPGVSQP VDQGGLGFGF
     KWNMGWMNDT LEYMKTDPLY RTHHHHKMTF GLVYAFSENF ILPISHDEVV HGKGSMLGKM
     PGNEWEKFAN LRAYYGFMWG HPGKKLLFMG QELAQRSEWN HDAQVDWDCL SNPQHAGMQA
     LVRDLNTLYR DTPALYARDC FESGFEWIIG DDQTNSVFAW IRHGNDGDPD VVVICNMTPQ
     EHGSYRVGMP AKGRWREALN SDSELYGGGN RGNYGGVDAK DGTHHGQPAY ADVTLPPLSA
     IYLVHEG
//
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