ID S7X3Y5_9FLAO Unreviewed; 636 AA.
AC S7X3Y5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=ADIWIN_1361 {ECO:0000313|EMBL:EPR73724.1};
OS Winogradskyella psychrotolerans RS-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR73724.1, ECO:0000313|Proteomes:UP000014962};
RN [1] {ECO:0000313|EMBL:EPR73724.1, ECO:0000313|Proteomes:UP000014962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR73724.1,
RC ECO:0000313|Proteomes:UP000014962};
RX PubMed=23950132;
RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT Ocean.";
RL Genome Announc. 1:e00630-e00613(2013).
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:EPR73724.1}.
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DR EMBL; ATMR01000089; EPR73724.1; -; Genomic_DNA.
DR RefSeq; WP_020897929.1; NZ_ATMR01000089.1.
DR AlphaFoldDB; S7X3Y5; -.
DR STRING; 641526.ADIWIN_1361; -.
DR PATRIC; fig|641526.4.peg.1351; -.
DR eggNOG; COG0296; Bacteria.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000014962; 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; 1.
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:UP000014962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 157..505
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 368
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 636 AA; 73875 MW; 9AF4617756A4DFE6 CRC64;
MGEVIAHSRF TDFDINLFKS GKHYRLYENF GSHITTLDGV EGVYFAVWAP SAKMVSVIGD
FNFWTEGEHK LNVRWDSSGI WEGFIPGAGK GSKYKYKILS SNNDIKTEKA DPYARRAEHN
PNTASIVWDD NYKWKDTKWM KKRKKNNALD APFSVYEVHL GSWKKKIEEN RFLSYVEMAD
ELVSYVKDMN FTHVELMPIM EFPYDPSWGY QVTGYFAPTS RFGYPEEFKL LVDKLHQNDI
GIILDWVPSH FPEDAHGLGL FDGSALYEHP DKRKGYHQDW KSLIFNYGRN EVKSFLISNA
IFWLDQYHAD GFRVDAVASM LFLDYSREDG EWEPNMFGGR ENLEAMSFLR EMNEAVYSAF
PDVQTIAEES TAFPMVSKPV SIGGLGFGMK WMMGWMHDTL QYFSKESVYR KFHQNDLTFS
MTYAFTENFM LPLSHDEVVY GKSSMLGKMP GDEWQRFANL RLLYSYMFTH PGTNLLFQGA
EFGQSGEWDF KTSLDWHLLQ YDPHQGVQQL VKDLNALYVK EPALHQKQFE AEGFEWIDYG
DSENSVFTYI RKGNEEKDDV IIACNMTPVP KENYKIGVPR KGKLKEIFNS DLKKYFGTGQ
YKNKINKTKA DAWHFRDNSV DIDIPPLGMV AFRYAK
//
