ID A0A2S5X6C7_9MICO Unreviewed; 734 AA.
AC A0A2S5X6C7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN ORFNames=C5C17_09715 {ECO:0000313|EMBL:PPG40113.1};
OS Pseudoclavibacter sp. RFBA6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pseudoclavibacter.
OX NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG40113.1, ECO:0000313|Proteomes:UP000237697};
RN [1] {ECO:0000313|EMBL:PPG40113.1, ECO:0000313|Proteomes:UP000237697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RFBA6 {ECO:0000313|EMBL:PPG40113.1,
RC ECO:0000313|Proteomes:UP000237697};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPG40113.1}.
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DR EMBL; PSUA01000011; PPG40113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5X6C7; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000237697; Unassembled WGS sequence.
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; 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; 2.
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 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; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000237697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 263..616
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 466
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 734 AA; 82127 MW; CB2D59502009F3E0 CRC64;
MTDELQPAAP VTTSIPDGEL RAVADGTHSG PHAILGQHLQ GDGRTVIRAR RPLAERVTAI
LTSSGERVEL HHLAHGIWQG AHEHGLDDYQ IETVYTDGVP HTVDDPYRFL PVVGEVDQFL
FGEGRHERLW HVFGAHHREH WGTHAPVRGT SFVVWAPHAQ AVRVIGSFNG WDGRAHAMRR
LDALGIWELF VPGVSPHETY KFQIRTASGE WVEKADPLAL HAEQPPQTAS VIATPSTYEW
GDGDWMSARA QKDPHTGPMT TYELHAMSWR PGLGYRELAD QLVEYLDGLE FTHVEFMPLA
EHPFGGSWGY QVTGYYAPTS RLGSPDDLRY LIDRLHQAGY GVIMDWVPGH FPKDSFGLAE
FDGQALYEHA DPRLGEQLDW GTKVFNFGDS QVRNFLVANA LYWLEEFHID GLRVDAVASI
LYLDYSREEW VPNIHGGREN LEAIAFLQEV NATAYKLYPG IAMIAEESTS WAGVTKPTEW
GGLGFGLKWN MGWMNDSLRY VERDPIYRSH HQGDLTFSFV YAWSERFLLP ISHDEVVHGK
GSLYSKMPGD EWQKLAGTRL FLAYQWGHPG KQLLFMGQEF AQQTEWSESR GLDWWQLDNP
GHAGVQRLVG DLNRLAKNEG ALWQRDDDPA GMVWLSGDDA ANSVLAFARR GFDGSPDVAM
IFNFSNQVIS GYRLGLPHAG RWSEVLNTDA ETYAGSGAGN YGSVTTEETP SHGFAQSATV
TVPPLAAVWF KYEG
//
