ID A0A101C6F3_9ACTN Unreviewed; 545 AA.
AC A0A101C6F3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE Flags: Fragment;
GN ORFNames=ADL25_09850 {ECO:0000313|EMBL:KUJ50412.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ50412.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KUJ50412.1}.
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DR EMBL; LMWH01000064; KUJ50412.1; -; Genomic_DNA.
DR RefSeq; WP_059127286.1; NZ_LMWH01000064.1.
DR AlphaFoldDB; A0A101C6F3; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 92..452
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUJ50412.1"
FT NON_TER 545
FT /evidence="ECO:0000313|EMBL:KUJ50412.1"
SQ SEQUENCE 545 AA; 61988 MW; 5132FC7342916FE5 CRC64;
WDGTGHPMRS LGSSGVWELF VPGVGEGALY KYDITRPDGS RTLRADPLAR RTETPPNTSS
IVYASHHEWG DGEWLAHRAD TAVHRAPFSV YEVHLPSWRP GLTYRQLAAQ LPAYVKELGF
THVELMPVAE HPFGGSWGYQ VTGFYAPTAR LGGPDDFKYL IDALHRAGIG VLMDWVPAHF
PRDDWALAEF DGRALYEHQD PLRAAHPDWG TLEFDYGRRE VRNFLVANAV YWCEEFHIDG
LRVDAVASML YLDYSREPGQ WSPNEHGGRE NLDAVAFLQE MNATVYRRCP GVVTVAEEST
AWDGVTRATH HRGPSGFGGL GFGLKWNMGW MHDSLQYMSH EPVHRRYHHH EMTFSMVYAY
SENYVLPISH DEVVHGKRSL VSKMPGDWWQ QRANHRAYLG FMWAHPGKQL LFMGQEFAQG
AEWSETHGPD WWLLDPAYGA QADHRGVRDL VRDLNAVYLR TPALWQRDTE PSGFRWTVGD
AAEDNVFAFL RYDDEDTPVL AVSNFSPVVR HDYRLGVPDD IPAWHELLNT DLAKYGGSDI
HNPDP
//
