GLGB_PSEPK
ID GLGB_PSEPK Reviewed; 736 AA.
AC Q88FN1;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=PP_4058;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN69648.1; -; Genomic_DNA.
DR RefSeq; NP_746184.1; NC_002947.4.
DR RefSeq; WP_010954852.1; NC_002947.4.
DR AlphaFoldDB; Q88FN1; -.
DR SMR; Q88FN1; -.
DR STRING; 160488.PP_4058; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q88FN1; -.
DR EnsemblBacteria; AAN69648; AAN69648; PP_4058.
DR KEGG; ppu:PP_4058; -.
DR PATRIC; fig|160488.4.peg.4314; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; Q88FN1; -.
DR BioCyc; PPUT160488:G1G01-4323-MON; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000556; 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..736
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188731"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 736 AA; 82877 MW; C43AFBAEE689D94E CRC64;
MNVTTRENGG LRQRDLDALA RAEHADPFAV LGPHGDGAGG QVVRAFLPNA LKVRIQARDD
GRVLAEMEQG SLPGLFSAHL DKAQPYQLHI VWAGGEQVTE DPYSFGPQLG DMDLHLFAEG
NHRDLSGRFG AQPTQVDGID GVCFSVWAPN ARRVSVVGDF NNWDGRRHPM RLRHGAGVWE
LFIPRLGVGE TYKFEVLGKD GILPLKADPL ARATELPPST ASKVAGELSH AWQDHDWMAQ
RAQRHAYNAP LSIYELHPGS WRCELDEAGE IGRFYNWREL AERLVPYVQE LGFTHIELLP
IMEHPFGGSW GYQPLSMFAP TSRYGSAEDF AAFIDACHQG GIGVLLDWVP AHFPTDEHGL
ARFDGTALYE YDNPLEGYHQ DWNTLIYNLG RNEVRGFMMA SALHWLKHFH IDGLRVDAVA
SMLYRDYSRK AGEWVPNRHG GRENLEAIDF IRHLNGVAAH EAPGALIIAE ESTAWPGVSQ
PTQQGGLGFA YKWNMGWMHD TLHYIQNDPV HRTYHHNEMS FGLIYAYSEH FILPISHDEV
VHGKHSLIDK MPGDRWQKFA NLRAYLTFMW AHPGKKLLFM GCEFGQWREW NHDAELDWYL
LQYPEHQGVQ RLVGDLNRLY REEPALHEQD CQPQGFQWLI GDDAQNSVYA WLRWSSSGEP
VLVVANFTPV PREGYRIGVP FGERWQELLN SDAELYAGSN VGNLGAVASD EVASHGQPLS
LALNLPPLGV LIMKPA
