ID A0A2T0RYF3_9RHOB Unreviewed; 737 AA.
AC A0A2T0RYF3;
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=CLV78_101156 {ECO:0000313|EMBL:PRY26063.1};
OS Aliiruegeria haliotis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=1280846 {ECO:0000313|EMBL:PRY26063.1, ECO:0000313|Proteomes:UP000239480};
RN [1] {ECO:0000313|EMBL:PRY26063.1, ECO:0000313|Proteomes:UP000239480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29328 {ECO:0000313|EMBL:PRY26063.1,
RC ECO:0000313|Proteomes:UP000239480};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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.
CC {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-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:PRY26063.1}.
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DR EMBL; PVTD01000001; PRY26063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RYF3; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000239480; 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; 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 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:UP000239480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 256..618
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 468
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 737 AA; 82378 MW; 6CEA362F68672ED0 CRC64;
MTNAPAKYPQ MPLSYETAEQ IAAGALGDPF AVLGPHESGG DIWVTTYDPG AVAMSALMNG
DEHPLDAFEG VAGVFCGKVP HKSPYLLRGR NAAGETWENE DPYRFGPVIG EMDEYLLAEG
THQRIWQVLG AHVMEHEGVE GTHFAVWAPN AKRVSVVCDF NAWDGRRNPM RLRGQTGVWE
IFLPGVGEGA VYKYEIIGAQ GQLMAQKADP VGFGAQHPPE TASMVRDISG YGWDDGKWMT
SREAANAHDA PISVYEVHLG SWKRVTDDGN RPLSYKEAAV ELVDYAKEMG FTHIEFLPVS
EFPFDGSWGY QPIGLFAPTV RHGPPHEFRD LIDAAHQAGI GVILDWVPGH FPTDVHGLAQ
FDGTALYEHA DPREGFHQDW NTLIYNYGRI EVANFLISNA LYWLEEYHID GLRVDAVASM
LYRDYSREEG QWIPNKDGGR ENYEAIAMLQ RTNSICYAEV PGIMTAAEES TSFPGVSKPV
DSGGLGFGFK WNMGWMNDTL DYISREPVHR KHHHHQMTFG IHYAFSENFI LPISHDEVVH
GKGSMIAKMP GLEGEKFANL RAYYGFMWGH PGKKLLFMGN EIAQWSEWNN NDQVDWKATE
YHTHAGVQRL VKDLNHLYRE TPALYAKDCE PGGFEWLEAN DMDHSVYAWI RRGGPEDPEV
VVICNFTPME RSAYRVGFPT PGTWREALNT DAGIYGGEGR GNLGSIQTEE KDWHGQDHSA
ALTIPPLSTI IFVRDDA
//
