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Database: UniProt
Entry: A0A1H0RMY0_9ACTN
LinkDB: A0A1H0RMY0_9ACTN
Original site: A0A1H0RMY0_9ACTN 
ID   A0A1H0RMY0_9ACTN        Unreviewed;       753 AA.
AC   A0A1H0RMY0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=SAMN04515671_3660 {ECO:0000313|EMBL:SDP30719.1};
OS   Nakamurella panacisegetis.
OC   Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC   Nakamurella.
OX   NCBI_TaxID=1090615 {ECO:0000313|EMBL:SDP30719.1, ECO:0000313|Proteomes:UP000198741};
RN   [1] {ECO:0000313|EMBL:SDP30719.1, ECO:0000313|Proteomes:UP000198741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4-7,KCTC 19426,CECT 7604 {ECO:0000313|Proteomes:UP000198741};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; LT629710; SDP30719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0RMY0; -.
DR   STRING; 1090615.SAMN04515671_3660; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000198741; Chromosome i.
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; 2.
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:UP000198741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          277..649
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        482
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   753 AA;  83160 MW;  871DBEBC7E3B661D CRC64;
     MSSPSTSSEP GVPPVVSTPP VTPAAPIGPS IDEYEKLIGG DTHNPHGILG AHPQPDGSTV
     IRTLRHHAKS VTLLTEGTET PLEHVHGGVF AVTVPGPPTD YRLRVVYAGP DGDISYEVDD
     PYRWLPTLGD IDLHLIGEGR HEFLWTVLGA HVRSYDTPIG SVTGTSFAVW APSARGVRVT
     GDFDHWSGAG QPMRSLGSSG VWEVFLPDVG AGTRYKFQIL GQDGVWREKA DPMAFGAEIP
     PATASVVTTS SYTWTDDAWM EQRRAADHLA GPMSIYEIHA GSWRTDIGYR EMADALVADL
     AETGFTHLEF LPLAGHPFGG SWGYQVTSYY APDPRFGSPD DFRYLVDRLH QAGIGVILDW
     VPAHFPKDEW ALGRFDGTSL YEHADPRRGE QPDWGTFVFD FGRREVRNFL VANALYWLEE
     FHLDGLRVDA VASMLYLDYS RNAGEWLPNV YGGRENLDAV AFIQETNATV GKRVPGAMMI
     AEESTAWPGV TRPTYLGGLG FHLKWNMGWM HDTLGYIARD PIYRAWHHNE LTFSMMYAYT
     EQFVLPISHD EVVHGKSSLW GKIPGDEWQK AATLRAYYAY MWAHPGKQLL FMGQELGTPW
     EWSETVQVPW QLKDYPIHNG IRSLVGDLNR TYKATPALYT QDFKPEGFRW IDANDRDGNV
     LAFLRWGSDG SSLVCVVNFS PQPHAGYRVG LPFSGVWREA VNTDSAIYGG SGAGNMGAVV
     ASDQPWHGLP SSATLTVPPL GALWLVPESA PHG
//
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