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GLGB_CUPNH
ID   GLGB_CUPNH              Reviewed;         756 AA.
AC   Q0K0X8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=H16_B1559;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR   EMBL; AM260480; CAJ96346.1; -; Genomic_DNA.
DR   RefSeq; WP_010814545.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0K0X8; -.
DR   SMR; Q0K0X8; -.
DR   STRING; 381666.H16_B1559; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q0K0X8; -.
DR   EnsemblBacteria; CAJ96346; CAJ96346; H16_B1559.
DR   GeneID; 57647461; -.
DR   KEGG; reh:H16_B1559; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_4; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 227746at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008210; Chromosome 2.
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; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 2.60.40.10; -; 2.
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; 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   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;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..756
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_1000044994"
FT   ACT_SITE        425
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        478
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   756 AA;  83098 MW;  0AE35BE8875F370B CRC64;
     MTPAHGTQPG MLPGHEFEAL LGARHHDPFA VLGPHPDGDG TLVRACLPGA ASVQLTDAGG
     TPLAEMARLH GGGVFAARLP REYKGGAPDY RLRVQWSDGS GQCGADPYAF GLLLGELDLH
     LIAEGRHFEL GACLGAQWQR VDGIDGVRFA VWAPNARRVS VIADFNGWHP ARHPMRLRHP
     SGIWELFIPA ALGAQPGSRY KYDLLDPHGT ELPDKADPLA LATEAPPATA SVVAGPGQGA
     PPFAWHDADW MARRGGADPY AAPMSVYEVH ALSWLRAAND TQRGWEILAE RLVPYVQELG
     FTHIELLPIT EHPFGGSWGY QPLSLYAPTA RLGPPQAFAA FIDRCHQAGI GVLLDWVPAH
     FPTDPHGLAR FDGTALYEHE DPREGFHQDW NTLIYNLGRN EVRGFLLAGA LHWLEHFHAD
     GLRVDAVASM LYRDYSREPG QWVPNRFGGR ENLEAIDFLR ELNAVVHERC PGALTIAEES
     TAWPGVTASV ASGGLGFDFK WNMGWMHDTL HYLGHEPVHR AWHHQDMTFG LVYAWSEAFV
     LPLSHDEVVH GKASMIGKVP GDEWQRFAGL RAYYGFMWAH PGKKLLFMGG ELAQWQEWNH
     DAELDWALLD HPMHRGMHTL VRDLNRLYRE LPALHALDHR PEGFQWVVGD DNHNSVFAWL
     RRAGPYSREV VLVVVNMTPV PRYGYRLGVP YAGAWQECLN TDAAVYGGTN VGNSGAVAAV
     DVPSHGQPAS LALTLPPLAT LVLRFDPGGG IQGAST
 
 
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