ID A9NFL7_ACHLI Unreviewed; 620 AA.
AC A9NFL7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
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:ABX81147.1};
GN OrderedLocusNames=ACL_0529 {ECO:0000313|EMBL:ABX81147.1};
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81147.1, ECO:0000313|Proteomes:UP000008558};
RN [1] {ECO:0000313|EMBL:ABX81147.1, ECO:0000313|Proteomes:UP000008558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX81147.1,
RC ECO:0000313|Proteomes:UP000008558};
RX PubMed=21784942; DOI=10.1128/JB.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; CP000896; ABX81147.1; -; Genomic_DNA.
DR AlphaFoldDB; A9NFL7; -.
DR STRING; 441768.ACL_0529; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; acl:ACL_0529; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_4_0_14; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008558; 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:UniProtKB-UniPathway.
DR CDD; cd11322; AmyAc_Glg_BE; 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; 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 NCBIfam; TIGR01515; branching_enzym; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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 Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:ABX81147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008558};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABX81147.1}.
FT DOMAIN 155..502
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 620 AA; 72750 MW; 1817CAF4DEC45721 CRC64;
MGRYIKLAFT ESHANLYLLG KNYLAHQFLG AHLNKDDDGN IISTTFTVYA PNAKEVRLIA
DFNNYEGWKH VLTKIHPQGF WSITIPKDLE WATYKYEIHL KNGKISHKSD PFGYFSEVRP
SNASKVYDID GYHWKDHDWF KNKKKVYDQP MLIYEVHLGS WQRNNGQFRP YNEVVKDLID
HVKYNGFTHI ELMPVYEHPL DDSWGYQGTG FFAATSRFGS PKDLMYLIDQ CHQHGIGIIM
DWVLGHINKD DFGLFNFDGT YLYEYEDTFK RENITWGTAN LDFNKGITKS FMMSALTFWM
DYFHVDGFRI DAVSHLFYYL GDESNGINEE AIAFLKEISA HVFSKDETFI LSAEDSTAFP
LVTKPTFLGG IGFNYKWNMG FMNDVLSYFK LDPIYRKHNH DKLTFGLVYA FNEQFILPFS
HDEVVHLKGS LVSKMPGSYE QKFAHYRNLM TFYMTHPGKK LLFMGQEFAQ IAEWDFKKEL
DWNLLKFPIH DAFNRYFRDL AHVYKHHDAL YQKDHDPSGF KWLIVDHKDT SVFAYARYSD
NEVLVMVHNL TPNYYQSYEV GVPFEGTYEE ILNSNKDIYN GTNLYNGLPL KTYKEPRNGQ
PYHLKVQLSG LTSIIFKYKK
//
