ID H0QLF0_ARTGO Unreviewed; 1294 AA.
AC H0QLF0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:GAB13651.1};
GN ORFNames=ARGLB_047_00010 {ECO:0000313|EMBL:GAB13651.1};
OS Arthrobacter globiformis NBRC 12137.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB13651.1, ECO:0000313|Proteomes:UP000003828};
RN [1] {ECO:0000313|EMBL:GAB13651.1, ECO:0000313|Proteomes:UP000003828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB13651.1,
RC ECO:0000313|Proteomes:UP000003828};
RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL Submitted (DEC-2011) 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=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC EC=2.7.1.175; Evidence={ECO:0000256|ARBA:ARBA00001537};
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|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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:GAB13651.1}.
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DR EMBL; BAEG01000047; GAB13651.1; -; Genomic_DNA.
DR STRING; 1077972.ARGLB_047_00010; -.
DR eggNOG; COG0296; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000003828; 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; 3.90.1200.10; -; 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; IPR002575; Aminoglycoside_PTrfase.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040999; Mak_N_cap.
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; PF01636; APH; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF18085; Mak_N_cap; 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.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685};
KW Reference proteome {ECO:0000313|Proteomes:UP000003828};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 753..1134
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 476..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 905
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 958
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1294 AA; 140254 MW; BE0D12D094BC8D00 CRC64;
MTQTTLTPTL EQLLRDWLPA QRWFPVKSPD FTLAPVGGLV LEDPTRRAGL EVFLASVASK
TADGVSRTDV VQIPLSYRSQ PLPGAERALI GESDDAEMGH RWVYDAVHDP AFIAAWLDLI
RTEDAAGTAS GHLSGAGQPL PQASGTVRVL SGEQSNTSVI VDDGDSAAIV KFFRVLSAGR
NPEVEVGAAL SAARTSEVPA TLGWVTGEWY PQGQLPQGKP ASGGPARGEL AVAHEFLAGG
RDAWRLAVDA AAGGVDFTAE AHALGHATAT VHRRLAETLG VSAEAVPGGD IAPGVAQRVR
QTWAEAGPAV GPYEEALESL LSRLEGTPAG ALQRIHGDLH LGQILQVPGA GGGHDRWAIL
DFEGEPLRPI SERNFPDVPL RDVTGMLRSF DYAAGAAERE QPDVRVPESW VDDCTEAFLA
GYAEVTPGTV DRNSPLFVAL WLDKALYEVV YELRNRPGWL AIPVNAARRL LSTKSSGEPA
GAAAEGNKMT GSAHTDSPHA PLHVDAHTLS RVAAGEHHAP HSVLGAHLDN YGHVTIRTVK
HLAEAVNVVT QAGTVPMTHE AEGVWVAVLE PLQHGHVPDY RLEVTYEGAE PVTVDDPYRY
LPTVGEVDLH LIGEGRHEKL WTVLGAHVQH YKSSLGDIDG VSFAVWAPNA EAVRVKGDFN
AWDGRENSLR SLGSSGVWEL FIPGVPAGAC YKYEIKTKGG YWVEKADPLA FGTEVPPLTA
SRVVESHYQF QDADWMKERA ARDPHNSPMS VYEVHLGSWR LGLSYRELAK ELVDYVKWLG
FSHVEFMPVA EHPFGGSWGY QVTSYYAPTS RFGHPDEFRF LVDSLHQAGI GVILDWVPAH
FPKDNWALAQ FDGQPLYEHA DPNLGEHPDW GTLIFDFGRT EVRNFLVANA LYWLDEFHID
GLRVDAVASM LYLDYSREHG QWQPNRFGGR ENLEAISFLQ EANATVYKTH PGAVMIAEES
TAFPGVTAPT SQGGLGFGLK WNMGWMHDSL KYASEDPVNR KWHHGTVTFS MVYAFTENFL
LPISHDEVVH GKGSMLRKMP GDRWQQLANL RAFLGYQWAH PGKQLIFMGT EFGQEAEWSE
QHGLDWWLAD IPAHRGIQML LKDLNGLYRS TPALYARDNE PGGFQWINGA DADRNVLTFV
RWDTEGNPLV CAVNFSGGPH KDYALGVPST GAWTEVLNTD SAEYGGSGVL NGGTLTAEDE
GIDGQPATLT VTLPPLGAAY FRPAGANVIT TAAAARAKAT EAESIFAGPT AAETGRVESR
AAEARDAEPG VVEPRSAEPK GETGKSALPG GPLV
//
