GLGB_RHORT
ID GLGB_RHORT Reviewed; 740 AA.
AC Q2RR72;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Rru_A2576;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC23373.1; -; Genomic_DNA.
DR RefSeq; WP_011390326.1; NC_007643.1.
DR RefSeq; YP_427660.1; NC_007643.1.
DR AlphaFoldDB; Q2RR72; -.
DR SMR; Q2RR72; -.
DR STRING; 269796.Rru_A2576; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q2RR72; -.
DR EnsemblBacteria; ABC23373; ABC23373; Rru_A2576.
DR KEGG; rru:Rru_A2576; -.
DR PATRIC; fig|269796.9.peg.2685; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_5; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR PhylomeDB; Q2RR72; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001929; 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..740
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260692"
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 740 AA; 83075 MW; 602E7CD8400F4F6F CRC64;
MDPKAYSEAV AALVGARHSN PFAFLGPHEG RAEGGRGGFC IRCFRPKATA VSLISAADDT
VLGRMKRLHP DGLFGIDLPE APGALAYRLR VSEGDEDRDI EDPYRFGPVL GELDRHLLGE
GTHLDIYRKM GAHPMTRDGV RGTGFALWAP NATRVSVIGD FNGWDGRLHP MRAHPGSGVW
DIFLPGVVEG HLYKYELLGP DGSLLPAKAD PYAFQAEKPP HTASVVRGLG TYAWNDGRWM
SERADRVATS APVSIYEVHL GSWRHGGGDR SLSYREMAEQ LIPYVKEMGF THIELLPVSE
FPFDGSWGYQ PIGLFAPTSR FGEPDDFRHF VDRCHQEGVG VILDWVAGHF PEDAHGLSWF
DGTHLYEHSD PRQGRHMDWG TYIFNYGRNE VRNFLLANAL FWLEQFHIDG LRVDAVASML
YLDYSRKAGE WVPNKFGGRE NLEAIDFLRR MNELVYGRFP GAVTIAEEST AWPMVSRPVH
LGGLGFGYKW NMGWMNDTLS YMSQDPIYRR FHQHDLSFGL LYAFTENFVL PLSHDEVVHG
KRSILGRMPG DAWQQFANLR AYYGFMWTHP GKKLLFMGCE FAQGREWNHN ASLDWHLLDI
DWHKGVQALV RDLNGLYAGV PALHDRDTEG YGFSWIDCTD ADQSVLAFLR FGETAEDVVM
VVCNFTPNPR HGYRLGAPIA GRWREIFNTD SAHYGGSNMG NSVVETEETK SHGHAQSVVL
TLPPLATIVL RPDGPITRIA
