ID E7N216_9FIRM Unreviewed; 807 AA.
AC E7N216;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
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 ECO:0000313|EMBL:EFW29798.1};
GN ORFNames=HMPREF9555_01026 {ECO:0000313|EMBL:EFW29798.1};
OS Selenomonas artemidis F0399.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=749551 {ECO:0000313|EMBL:EFW29798.1, ECO:0000313|Proteomes:UP000004633};
RN [1] {ECO:0000313|EMBL:EFW29798.1, ECO:0000313|Proteomes:UP000004633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0399 {ECO:0000313|EMBL:EFW29798.1,
RC ECO:0000313|Proteomes:UP000004633};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFW29798.1}.
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DR EMBL; AECV01000016; EFW29798.1; -; Genomic_DNA.
DR RefSeq; WP_009349692.1; NZ_GL638136.1.
DR AlphaFoldDB; E7N216; -.
DR STRING; 749551.HMPREF9555_01026; -.
DR HOGENOM; CLU_004245_4_1_9; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000004633; 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; 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 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|HAMAP-Rule:MF_00685,
KW ECO:0000313|EMBL:EFW29798.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 153..508
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 653..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 363
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 807 AA; 91648 MW; FEF7E57CEDE74BCA CRC64;
MKTSALSEFD LYLFHQGTNY HAQEMLGAHF LERDGKRGVR FAVWAPNAKA VSVVGAFNDW
NTLLNPMNRI ADGEIWETFV EGLGEGEIYK YAIEPQWGGP HIMKADPYGF YAEKKPQTAS
RTYDMTKYEW QDGAWQEQKA RETSYERPML TYEVHAGSWR RTLEGEYLSY HEMADQLIGY
VKDMNYTHIE FMPLCEHPYD GSWGYQATGY FAVTSRYGTP DDFRYLVDTA HQNGIAIIMD
WVPGHFCKDE QGLRRFDGKN LYESDNETRA ENREWGTTNF DYGRTEVQSF LISNALFWLE
EFHIDGLRID AVANMLYLNY GRRDGEWQPN KYGDTGNLEA MDFLKKLNET IFKYHPHALM
IAEESTSWPL ISKPVYMGGM GFNYKWNMGW MNDMLDYVSL DPIYRKWNQD KITFSLMYAF
SENFVLPLSH DEVVHGKRSL IEKMPGDYWQ KFAGLRGFFG YWIAHPGKKL LFMGGEFGHF
IEWNFDDSMD WHLVEQYPMH TKMLAYSKAL NKFYVENTCF WQVDFDWSGF QWIDCNDNEN
SIIALVRRAD DPSDFLVCVH NFTPEVHQGY RIGVPTKGTY VEVFNSDEEA YGGSGVVNAG
DLVSEDYAYH GREQSIVITV PPLASTFYRL KRQSGAGTPV SKLPEIADAV AKKKATSAQP
KAAAARKKSA AADEEAKPAP KKKGAVKAKA EIAAEEKPVP KKRTAAKRSA AADTDSVPAP
KKRESAKKST AESDADEKPA PKKTRTVKAK TEESAEEKPA PKKRAAAKKP AAEKVGAQGM
TAVKKKTVRK TAQGAEDAPQ KARSTKG
//
