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GLGB_VIBCH
ID   GLGB_VIBCH              Reviewed;         729 AA.
AC   Q9KNE8; Q9KNE9;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 2.
DT   03-AUG-2022, entry version 126.
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};
GN   OrderedLocusNames=VC_A0015/VC_A0016;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95929.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAF95930.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE003853; AAF95929.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE003853; AAF95930.1; ALT_FRAME; Genomic_DNA.
DR   PIR; D82511; D82511.
DR   RefSeq; WP_000705042.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KNE8; -.
DR   SMR; Q9KNE8; -.
DR   STRING; 243277.VC_A0016; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   DNASU; 2612506; -.
DR   EnsemblBacteria; AAF95929; AAF95929; VC_A0015.
DR   EnsemblBacteria; AAF95930; AAF95930; VC_A0016.
DR   GeneID; 57741491; -.
DR   KEGG; vch:VC_A0015; -.
DR   KEGG; vch:VC_A0016; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_2653510_0_0_6; -.
DR   BioCyc; VCHO:VCA0016-MON; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
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..729
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188759"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        461
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   729 AA;  84027 MW;  ECDE22002582E543 CRC64;
     MKITKKPSKV QQFYDQLARA AFADPFSFLG PYIPAEQGAL RVWMPGADNV ALVVEGQARV
     ALEREGEGGF VLKDGRNLRF THYQLAVDWA GTEQLLDDPY QYHGLYAEYE DLHTPKQMYH
     HMGAQFVTLE RDGKMVSGVR FLVYAPHAAA CSLIGAFNHW DGRRHPMQRL DYGIWGIFIP
     GLPEGTQYKF ELKGPHGEGL PHKADPWGFY AEQYPSFASV TYDHRRYQWQ DTAWQQRPVT
     EKRKQALSFY ELHVGSWKRG ENGEFLNYRE LADQLVPYLV EMGYTHVELM PVAEHPFYGS
     WGYQPVGLFA PTSRYGSPDD FKYFVDLCHQ AGIGVVLDWV PAHFPSDSHG LANFDGTPLF
     HDPDPRRGWH QDWNSYIYDL GREHVRRFLV ANALYWFEMF HIDGIRVDAV ASMLYLDYSR
     SHDQWIPNVD GGRENYDAIA TFKWMNEEVY KHFPNAMTIA EESTAFPGVS APTFMGGLGF
     GFKWNMGWMH DSLSYIKEDP VHRKYHHNTL TFPLIYAFSE NYVLSLSHDE VVYGKRSLMY
     KMPGDEWQQT ANLRAYLGYM YGQPGKKLNF MGTELGQTAE WDHDGQLQWF LTQFERHAGI
     QRLVRDLNHL YQAQTALHQL DCDPRGFEWR LQDNADLSVI AHERMDEAGN RVLVITNFTP
     VPQQEFRLGV PKTGKYRLLL NTDAKQYNGS DYPVLQDVST EAISSEGLDQ SLLLSVPPLA
     TLFYQWSAK
 
 
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