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GLGB_PICTO
ID   GLGB_PICTO              Reviewed;         705 AA.
AC   Q6L2Z9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=PTO0067;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42652.1; -; Genomic_DNA.
DR   RefSeq; WP_011176868.1; NC_005877.1.
DR   AlphaFoldDB; Q6L2Z9; -.
DR   SMR; Q6L2Z9; -.
DR   STRING; 263820.PTO0067; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAT42652; AAT42652; PTO0067.
DR   GeneID; 2844042; -.
DR   KEGG; pto:PTO0067; -.
DR   PATRIC; fig|263820.9.peg.80; -.
DR   eggNOG; arCOG02951; Archaea.
DR   HOGENOM; CLU_004245_4_0_2; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 2860at2157; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000438; 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; cd02855; E_set_GBE_prok_N; 1.
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; 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; 1.
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..705
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188772"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        446
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   705 AA;  82273 MW;  5816875946D2A5C0 CRC64;
     MIKLYNTCMD FKCLNDVECS HPEKILGPHL EDAYIIRAYI PIARAAFILI DNKKYQMIDN
     GKVFEYRSDN EINDYKILYI DDSGYEKTID DPYRFRPEIS DYDIYLYGTG RLFEAYKTFG
     AHLKTIKDVS GCNFVVWAPS ALSVSVVGNF NHWTPGMHPM INVNDSGIWA LFIPGIKENE
     VYKFAIKTKN NEIKMKTDPF AFYTEKRPRT GSIVINDDFH WTDNSFKRSE NALSIYEMHL
     GSWKRNNGDY YNYREIADML IDHLKKTGFN CVEIMPVMEH PLDISWGYQV VNYFAPTSRY
     GKPDDFKYLV NRLHENNIMV ILDFVPAHFP DDDYGLYMFD GTHLYDYEDP RMGRTPDWGT
     NIFDFGRNGV RSFIASAAVF WIDKYHVDGL RFDAVTSMIY LDFGRKPGEW IPNINGGNIN
     LEAVSLLKEI NDYIHNKYYN VITVAEESST YPGITSESGL NFNYKWNLGW MHDTLDFFHE
     DPLYRKYRIN NLTFSVMYMY SENFILPVSH DEVVYGKGSL YRKMPGNKNE KISNVKLFLS
     YMFSYPGKKL LFMGNEFAQK NEWNVLSQLS WNDLDDGKYV MELIHDLNNL YKNDFNFYND
     KNFSWIDFND KTNTVISFNR GNAVCIFNFT PVERENYAIG VDYPSRYIEI INTDSKKYNG
     GNILNESIYA CKYPMHGRRY SIEIDLPPLA AVIMEPEDLN GSSGN
 
 
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