GLGB_CHLTB
ID GLGB_CHLTB Reviewed; 738 AA.
AC B0BAX7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=CTLon_0241;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; AM884177; CAP06639.1; -; Genomic_DNA.
DR RefSeq; WP_012263574.1; NC_010280.2.
DR AlphaFoldDB; B0BAX7; -.
DR SMR; B0BAX7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; ctl:CTLon_0241; -.
DR HOGENOM; CLU_004245_3_2_0; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000794; 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..738
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000131814"
FT ACT_SITE 399
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 452
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 738 AA; 84578 MW; 190F260680D5910F CRC64;
MDPFFLNTQH VELLVSGKQS SPQDLLGIVS ESLNQDRIVL FRPGAETVFV ELRGKIQQAE
SHHSGIFSLP VMKGISPQDY RVYHQNGLLA HDPYAFPLLW GEIDSFLFHE GTHQRIYERM
GAIPCEIDGV PGVRFIVWAP HAQRVSVIGD FNGWHGLVNP LHKVSDQGVW ELFVPGLTAG
ACYKWEMVTE SGQVLIKSDP YGKFFGPPPR SVSVVIDDSY EWNDSEWLEE RIKKTEGPMN
IYEVHVGSWQ WQEGQPLNYK ELADQLALYC KQMHYTHVEL LPVTEHPLNE SWGYQTTGYY
APTSRYGSFE DLQYFIDTMH QHGIGVILDW VPGHFPIDSF AMSGFDGTPL YEYTRNPSPL
HPHWHTYTFD YAKPEVCNFL LGSALFWIDK MHVDGIRVDA VSSMLYLDYG RYAGEWVPNR
YGGRENLDAI RFLQQFNTVI HEKYPGVLTF AEESTTFPKI TVSVEEGGLG FDYKWNMGWM
HDTLHYFEKD FPYRPYHQSD LTFPQWYAFS ERFLLPFSHD EVVHGKRSLI GKMPGDAWRQ
FAQLRLLLGY QICQPGKKLL FMGGEFGQGR EWSPGRELDW ELLDISYHQG VHLCSQELNA
LYVQSPQLWQ ADHLPSSFRW VDFSDVRNGV VAYLRFADAD AKKALLCVHH FGVGYFPHYL
LPILPLESCD LLMNTDDTRF GGSGKGFREP EILTPEIARQ EREAAGLIEA DDESGPDCWG
LDIELPPSAT LIFSVTLQ
