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Database: UniProt
Entry: F4CKW7_PSEUX
LinkDB: F4CKW7_PSEUX
Original site: F4CKW7_PSEUX 
ID   F4CKW7_PSEUX            Unreviewed;       832 AA.
AC   F4CKW7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   OrderedLocusNames=Psed_1725 {ECO:0000313|EMBL:AEA23960.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA23960.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA23960.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
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; CP002593; AEA23960.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CKW7; -.
DR   STRING; 675635.Psed_1725; -.
DR   KEGG; pdx:Psed_1725; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_11; -.
DR   OMA; FGMKWMM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000007809; Chromosome.
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:UP000007809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          275..616
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..791
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        427
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   832 AA;  91331 MW;  DF0915971CD0610C CRC64;
     MGHYGSRVDR EDTNTRTIGA GTADSHAPDP RTVDRLLGGA HHNPHGVLGA HQGRDGTIVR
     TLRPHADEVS VLLHGDTDRS FPLTRVHEAG LFSGIVPGEP DDYRLAVRYG EDTHVVDEPY
     RWLPTLGEVD LHLIAEGRHE RLWDVLGSHV RTYDTASGQV TGTSFAVWAP TAQGVRVTGD
     FDGWAGWAHP MRSLGSSGVW ELFVPDVGVG TRYKYRILGQ DGRWRDKADP MAFATEIPPA
     TASVVTATTH EWGDTDWMTA RAGRRPHAEP MSVYEMHLGS WRPGLGYREL AQELVEYLSE
     TGFTHVELLP VAEHPFGGSW GYQVTSYYAP TARFGSPDDF RYFVDTLHQA GYGVIVDWVP
     AHFPRDEWAL ARFDGGPLYE HADPRRGEQP DWGTLVFDFG RREVRNFLVA NALFWCEEFH
     IDGLRVDAVA SMLYLDYSRA DGQWLPNIHG GRENLDAVAF LQEMNATVYR NHPGVVTIAE
     ESTAWPGVTR PTHLGGLGFG FKWNMGWMHD TLDYTGRDPI HRSYHHNQMT FSLMYAFSEN
     YVLPLSHDEV VHGKGSLWTR MPGDDWNKAA GVRALLAFMW AHPGKQLLFM GGEFGQVREW
     SEQRPLDWHL LEDPLHGGIR TLLGDLNRAY RSQPALWALD TTPAGFSWID ANDASGNVLS
     FLRMSGTETG DDGTPNVLAC IANFSGTPNE NYRVGLPFAG RWRELVNTDA EAYGGSGVGN
     LGFVEAEQRS WHGRPASAVL RLPPSGVLWL VPDNSGGPVH RGSLTAGAPP APTPVREPAV
     VAPPSSSRPA PLPAADPEAV SEARDIEPPA PGPADANGGR AGTGASGPPP QG
//
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