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GLGB_MYXXD
ID   GLGB_MYXXD              Reviewed;         734 AA.
AC   Q1D654;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=MXAN_3682;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(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; CP000113; ABF92763.1; -; Genomic_DNA.
DR   RefSeq; WP_011553700.1; NC_008095.1.
DR   AlphaFoldDB; Q1D654; -.
DR   SMR; Q1D654; -.
DR   STRING; 246197.MXAN_3682; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABF92763; ABF92763; MXAN_3682.
DR   GeneID; 41361017; -.
DR   KEGG; mxa:MXAN_3682; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_7; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 227746at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002402; 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; -; 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..734
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260668"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        467
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   734 AA;  83383 MW;  708A85B24C81DD25 CRC64;
     MRKPADKAQV DAELQRVVEL RHPEPHAVLG IHPDGDGVVI RAFRPDAVAI HVLPESGGRV
     AMTHRPGGVY EARINGKDQT FNYLLEVEYP GKRVFTLRDP YSFLPTLGEM DLYYAGEGRH
     ERLWERMGAH LLHHHGVRGT SFAVWAPTAA GVSVVGDFNG WDGRLHSMRR MGSSGIWELF
     VPEVGEGTRY KFEIRPGQGG PNVLKADPFA FRTEVPPATA SVVHDLARYT WGDAAWLEQR
     AQRRDVHHQP WSVYEVHLGS WRRVVEDGDR PMTYRELAPA LAEYIKFTGF THIELLPVAE
     HPYGGSWGYQ VGGYYAPTAR FGHPDDLRFF IDHMHQEGIG VLVDWVPGHF PRDLHALGQF
     DGTALYEHAD PRKGAQPDWG TLVFNFGRNE VRNFLIANAL FWIEEYHIDG LRVDAVASML
     YLDYSRKQGE WIPNRWGGRE NEEAIHFLRE LNETVHRKHP GVVVIAEEST AWPKVSAPVS
     EGGLGFDYKW NMGWMHDTLS YFSKDPIYRQ YHHNQLTFGL LYAFSEQFML PLSHDEVVHG
     KGSLYGRMPG DPWQKRANLR ALFAWMWAHP GKKLVFMGGE FGQPAEWNHD KSLDWHLTHD
     PGHHGILQLV SDLNRIYRDM PALHDADGEP MGFQWLQPDS AAYNVFAFVR RARQPGRHVV
     CIANLSPTVR ENYRVGFPFQ GRYVELLNTD AEQYGGSNLG NMGQIHTEPT GWDGQPASAT
     LTLPPLSVLW FTPG
 
 
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