(data stored in SCRATCH zone)

SWISSPROT: D1CE93_THET1

ID   D1CE93_THET1            Unreviewed;       731 AA.
AC   D1CE93;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 76.
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   OrderedLocusNames=Tter_0327 {ECO:0000313|EMBL:ACZ41249.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41249.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41249.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:
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|HAMAP-Rule:MF_00685,
CC         ECO:0000256|SAAS:SAAS01115213};
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}.
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DR   EMBL; CP001825; ACZ41249.1; -; Genomic_DNA.
DR   RefSeq; WP_012874284.1; NC_013525.1.
DR   STRING; 525904.Tter_0327; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACZ41249; ACZ41249; Tter_0327.
DR   KEGG; ttr:Tter_0327; -.
DR   eggNOG; ENOG4107R91; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000283037; -.
DR   KO; K00700; -.
DR   OMA; NLKWNMG; -.
DR   OrthoDB; 227746at2; -.
DR   BioCyc; TTER525904:G1GGS-331-MONOMER; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000323; 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   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; 2.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CE93.
DR   SWISS-2DPAGE; D1CE93.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956847};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
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:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00685,
KW   ECO:0000256|SAAS:SAAS00956835}.
FT   DOMAIN      254    616       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    411    411       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00685, ECO:0000256|PIRSR:PIRSR000463-
FT                                1}.
FT   ACT_SITE    464    464       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00685, ECO:0000256|PIRSR:PIRSR000463-
FT                                1}.
SQ   SEQUENCE   731 AA;  84819 MW;  B533E3C00366A62C CRC64;
     MQIEGACRIE DLINGTCYDP HSILGMHPVE RNGRRCIELR VWVPGAIKVS ALDYKTNEEI
     LPLERVHEAG FFIGTFPTRT EVFPYRLRIS TAHHTWVQED PYRFLPTIGE LDLYYIGEGT
     HRKLYEVLGA HLREIDGVKG VSFAVWAPNA RGVSVIGDFN GWDKRRYPMR VLGSSGVWEI
     FLPGVQVGEK YKYAINGADG IEREKADPLA FYSELRPRTA SIIYDLSGYK WKDREWMLRR
     LENNPYKKPM NIYEVHLGSW KRHPDGSWLS YRELADELVP YVKRMGFNYV EFMPLLEHPY
     DGSWGYQVTG FYSATSRFGT PDDLRYLIDR CHQAGIGVII DWVPAHFAVD EHGLCRFDGT
     YLYEHEDIRR RFQPDWGTFS FNYGRNEVRN FLTASALFWV KEFHVDGLRV DGVSSMLYLD
     YSRGPGEWTP NKYGGRENLE AIDFLREMNS LVYAEGEGAI TIAEESTAWP GVSRPVYLGG
     LGFGFKWNMG WMHDTLEYFR KDPIYRKYHH NDLTFSMVYA YNENFILSLS HDEVVHGKGS
     LVNKMPGDEW QQFANLRLLF AYQWAHPGKK LIFMGDEFGQ RSEWNHDWQL DWWVLQFGYH
     QGVQRLLQDL NRLYLHEPAL YRLDHDPKGF TWLDYSDWEN SVISFARWSG DGNNHIVCAF
     NFTPVPRYNY RIPAPHLGKY REVLNTDAQI YGGSGIGNMG EVSSEVVMHN GHPYSVAITL
     PPLGAVFFKP M
//

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