GenomeNet

Database: UniProt
Entry: A0A0A0C5Y4_9CELL
LinkDB: A0A0A0C5Y4_9CELL
Original site: A0A0A0C5Y4_9CELL 
ID   A0A0A0C5Y4_9CELL        Unreviewed;       734 AA.
AC   A0A0A0C5Y4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   28-FEB-2018, 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=N867_03675 {ECO:0000313|EMBL:KGM16033.1};
OS   Actinotalea fermentans ATCC 43279 = JCM 9966 = DSM 3133.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Actinotalea.
OX   NCBI_TaxID=862422 {ECO:0000313|EMBL:KGM16033.1, ECO:0000313|Proteomes:UP000029877};
RN   [1] {ECO:0000313|Proteomes:UP000029877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3133 {ECO:0000313|Proteomes:UP000029877};
RA   Chen F., Li Y., Wang G.;
RT   "Actinotalea ferrariae CF5-4.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic
CC       linkages in glycogen by scission of a 1,4-alpha-linked
CC       oligosaccharide from growing alpha-1,4-glucan chains and the
CC       subsequent attachment of the oligosaccharide to the alpha-1,6
CC       position. {ECO:0000256|HAMAP-Rule:MF_00685,
CC       ECO:0000256|SAAS:SAAS00077459}.
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       chain to a primary hydroxy group in a similar glucan chain.
CC       {ECO:0000256|HAMAP-Rule:MF_00685, ECO:0000256|SAAS:SAAS00956848}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00685, ECO:0000256|SAAS:SAAS00956853}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685,
CC       ECO:0000256|SAAS:SAAS00956854}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00685,
CC       ECO:0000256|SAAS:SAAS00956845}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGM16033.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AXCX01000140; KGM16033.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGM16033; KGM16033; N867_03675.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000029877; 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   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 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; 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   PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956847};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029877};
KW   Glycogen biosynthesis {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956838};
KW   Glycogen metabolism {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956840};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956843};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029877};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956835}.
FT   DOMAIN      258    639       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    410    410       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00685, ECO:0000256|PIRSR:PIRSR000463-
FT                                1}.
FT   ACT_SITE    463    463       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00685, ECO:0000256|PIRSR:PIRSR000463-
FT                                1}.
SQ   SEQUENCE   734 AA;  81872 MW;  8748C4F61F52BD0A CRC64;
     MTTSPEPTAR PTPVDTAELD AIAKGLHQDP HRVLGPHLSE GTVTIRLLRP LADEVEVVTP
     TGSVPATHEH GGVWLATMPG AQVPDYRVRV RYGDHVDLQD DPYRFLPTLG EVDLHLISEG
     RHEELWTVLG ANVRTYPSVL GEVVGTSFAV WAPNAAAVRV VGDFNHWQGT PHTMRNLGSS
     GVWELFVPGV RGGQRYKFEI LAKDGSWRQK ADPLAKGTEH PPATASVVVE STHDWGDDAW
     LERRRSGNPH HGPMSVYEVH LGSWRPGLGY RDLAEELTEY AVSLGFTHVE LLPVAEHPFG
     GSWGYQVSSY YAPTSRFGHP DDFRHLVDRL HQAGIGVLLD WVPAHFPKDE WALGRFDGTP
     LYEHPDPLLG EQPDWGTYVF NFGRNEVRNF LVANATYWLE EFHVDGLRVD AVASMLYLDY
     SRGAGQWRPN IHGGRENLEA IRFIQEANAT AYRRTPGILM IAEESTAWPG VTAPTDAGGL
     GFGLKWNMGW MNDTLRYLAE EPINRRYHHH EATFSLVYAF SEHFVLPLSH DEVVHGKGSL
     VYKMPGDDWQ RFAGLRVLLA YQWSHPGKQL LFMGGEFGQT AEWSEGRSLD WHLLEYGPHQ
     GVQRLVTDLN RFYRTEPALW DLDDEPAGFE WIDSQDAGHN VLSYVRRDRS GRMVAVVVNF
     AGTTHEGYLL GLPAAGGWRE ALNTDAEHYG GSGVGNLGRV EAEPVLQHAQ PASVRLRVPP
     LAALFLVPEG QPDL
//
DBGET integrated database retrieval system