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GLGB_PSEU2
ID   GLGB_PSEU2              Reviewed;         741 AA.
AC   Q4ZTJ2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=Psyr_2491;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY37530.1; -; Genomic_DNA.
DR   RefSeq; WP_011267721.1; NC_007005.1.
DR   RefSeq; YP_235568.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZTJ2; -.
DR   SMR; Q4ZTJ2; -.
DR   STRING; 205918.Psyr_2491; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q4ZTJ2; -.
DR   EnsemblBacteria; AAY37530; AAY37530; Psyr_2491.
DR   KEGG; psb:Psyr_2491; -.
DR   PATRIC; fig|205918.7.peg.2551; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   OMA; FGMKWMM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000426; 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; 2.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..741
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260680"
FT   ACT_SITE        420
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        473
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   741 AA;  84062 MW;  30571708F8CEEF0F CRC64;
     MNAPDKTGTR RRAIPAAVDL DALIRAEHRD PFSILGPHGD GGSGQYVRAY LPAALSVRLL
     ARDDGRELGE MEMSEVPGFF VGHLEHPQPY LLKINWAGGE QITEDPYSFG PLLGEMDLYL
     FAEGNHRDLS SCLGAQVTSV DGVDGVRFAV WAPNARRVSV VGSFNSWDGR RHPMRMRHPT
     GVWEIFVPRL QPGEVYKYEI LGAHGILPLK SDPMALSTTL PPDTASKIAA PLQFEWNDQE
     WLQSRAGRHE VTAPLSIYEL HAGSWQMEQV EDNQWRQYNW RELADRLIPY VKELGFTHIE
     LMPIMEHPFG GSWGYQLLAQ FAPTARYGSP EDFAFFVDAC HRAEIGVILD WVPAHFPTDT
     HGLAQFDGTC LYEYADPKEG FHQDWNTLIY NLGRTEVHGF MLASALHWLK HYHIDGLRVD
     AVASMLYRDY SRNAGEWVTN RFGGRENLEA IDFLRHLNDV VALEAPGTMV IAEESTAWPG
     VSEPTQQGGL GFNYKWNMGW MHDSLQYMEE DPINRGHHHG KLSFSLVYAW SERFVLPISH
     DEVVHGKHSL IDKMPGDRWQ KFANLRAYLS FMWTHPGKKL LFMGCEFGQW REWNHDRELD
     WYLMQYAEHV GVKNLVGDLN RLYREEKALH ERDADPAGFQ WLVGDDSANS VFAYLRWSND
     GEPLLVVANM TPVPRLDYRL GAPMRGAWTE LLNSDAETYA GSNFGNGGEV MTEAEPAHGM
     EDSLVLNLPP LAVLILKPKK D
 
 
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