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Database: UniProt
Entry: A0A1P8UZJ8_9RHOB
LinkDB: A0A1P8UZJ8_9RHOB
Original site: A0A1P8UZJ8_9RHOB 
ID   A0A1P8UZJ8_9RHOB        Unreviewed;       727 AA.
AC   A0A1P8UZJ8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=Ga0080574_TMP4452 {ECO:0000313|EMBL:APZ54786.1};
OS   Salipiger abyssi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1250539 {ECO:0000313|EMBL:APZ54786.1, ECO:0000313|Proteomes:UP000187059};
RN   [1] {ECO:0000313|EMBL:APZ54786.1, ECO:0000313|Proteomes:UP000187059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2014 {ECO:0000313|EMBL:APZ54786.1,
RC   ECO:0000313|Proteomes:UP000187059};
RA   Tang K.;
RT   "Deep-sea bacteria in the southern Pacific.";
RL   Submitted (APR-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; CP015093; APZ54786.1; -; Genomic_DNA.
DR   RefSeq; WP_076704853.1; NZ_CP015093.1.
DR   AlphaFoldDB; A0A1P8UZJ8; -.
DR   STRING; 1250539.Ga0080574_TMP4452; -.
DR   KEGG; paby:Ga0080574_TMP4452; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000187059; 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; 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:UP000187059};
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;  81272 MW;  2FDD898D39F4B44B CRC64;
     MTDANHPTAP DFQRLINGHH DDPFSILGPH SQDGARSVTA FDPGAREMWA VIGDKPHPLA
     PVDGAPGVFR GKVPGDKPYF LRGAAGGNSW EFEDAYRFGP VLGEIDEYLL GEGSHLRLWE
     ALGAHVIEHE GVRGTQFAVW APNAKRVSVV GDFNWWDGLR HTMRRRGATG VWEIFVPAVG
     DGALYRYEIV GPDGQLQPHK SDPVGFGSEH PPANASIVRD IEGYGWSDGD WMTSRQAAQN
     REAPISVYEV HLPSWRRKDW GRPISYVEAA TELVDYVKEM GFTHIELLPI SEYPFDGSWG
     YQPIGMFAPT IRCGLPHEFR DLVNAAHRAG LGVILDWVPG HFPSDPHGLG KFDGTALYEH
     ADPREGFHKD WNTLIYNYGR AEVSNFLTAN ALYWLEEYHA DGLRVDAVAS MLYRDYSRQP
     GEWVPNKDGG RENYEAISLL QRMNTATYGE NPGIVTVAEE STAYPGVSQP VDQGGLGFGF
     KWNMGWMNDT LEYVKKDPVY RQYHHHQMTF GLVYAFSENF ILPISHDEVV HGKGSMIGKM
     PGSDWEKFAN LRAYYGFMWG HPGKKLLFMG QELAQWSEWN HDAQVDWDCL QNPAHAGIQA
     LVRDLNHLYR DTPALHAKDC YADGFQWICG DDAQNSVFSW VRRGAPGDPE VVVICNFTPQ
     EQGSYRMGMP ATGRWREALN SDAEIYGGGN RGNYGAVEAH AGDHHGQPAY ADVTIPPLST
     VYLIRDS
//
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