ID Q7UYJ7_RHOBA Unreviewed; 633 AA.
AC Q7UYJ7;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN Name=glgB {ECO:0000313|EMBL:CAD71645.1};
GN OrderedLocusNames=RB548 {ECO:0000313|EMBL:CAD71645.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD71645.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD71645.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000256|ARBA:ARBA00000826};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; BX294133; CAD71645.1; -; Genomic_DNA.
DR RefSeq; NP_863971.1; NC_005027.1.
DR AlphaFoldDB; Q7UYJ7; -.
DR STRING; 243090.RB548; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAD71645; CAD71645; RB548.
DR KEGG; rba:RB548; -.
DR PATRIC; fig|243090.15.peg.274; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_5_1_0; -.
DR InParanoid; Q7UYJ7; -.
DR OrthoDB; 226102at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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:InterPro.
DR CDD; cd11325; AmyAc_GTHase; 1.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000313|EMBL:CAD71645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAD71645.1}.
FT DOMAIN 161..517
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 363
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 633 AA; 72020 MW; 708ECC306CC9D9E7 CRC64;
MSFAMVDSLR RTVAQRLIVI EGREMEQTAL LDGMEENATE QSSVTKSGMG AIVHDDGVAF
RVWAPNADSV SVLGTFNQWK EDATPLKREE HGTWYVDVAD AKAGDEYKYR IIRGDKSYDR
IDPYAREVTN SIGNAVVYAD TFDWKHPTFD RPAQNELVIY EMHIGTFHRD DPDQPGTFSD
AVAKFKHLKE LGVNAIQIMP VAEFAGDLSW GYNPAHIFAV EQAYGGPDAL KAFVDAAHEA
GFAVIIDVVY NHFGPSDLDL WQFDGWSEND KGGIYFYQDH RSNTPWGDTR PDYGRGEVRQ
FIHDNAMMWM REYHADGLRY DMTAYIRTIS GIGDDDIAEG WGLMQWINRD LRNEFPGCYL
IAEDLQTNNW LTKTEDQGGA GFTTQWDAAF VHPIRSAVQE IDDAHRDMWA VRDALCHRYN
GDAFQRVIYS ESHDEVANGK SRVPSEIDAE DPESRFAKKR TILAAALALT APGVPMLFQG
QEMLEDDWFE DTDPLEWERT RRLKGIKRLF RDLIHLRLNN DGLSKGLTGQ HIVMHHVNEN
DKVVAFVRRA EDPQDDVVVL ANFANRSWDQ YEIGFPDSGD WQLKLNTDWS GYDQDFDDHP
VEHVDATEQP YDGLAARAEV SFGAYAVLVY TRK
//
