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Database: UniProt
Entry: A0A142WXC1_9PLAN
LinkDB: A0A142WXC1_9PLAN
Original site: A0A142WXC1_9PLAN 
ID   A0A142WXC1_9PLAN        Unreviewed;       654 AA.
AC   A0A142WXC1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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_2 {ECO:0000313|EMBL:AMV19244.1};
GN   Synonyms=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN   ORFNames=VT03_15240 {ECO:0000313|EMBL:AMV19244.1};
OS   Planctomyces sp. SH-PL14.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV19244.1, ECO:0000313|Proteomes:UP000076318};
RN   [1] {ECO:0000313|EMBL:AMV19244.1, ECO:0000313|Proteomes:UP000076318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV19244.1,
RC   ECO:0000313|Proteomes:UP000076318};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) 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; CP011270; AMV19244.1; -; Genomic_DNA.
DR   RefSeq; WP_075093737.1; NZ_CP011270.1.
DR   AlphaFoldDB; A0A142WXC1; -.
DR   STRING; 1632864.VT03_15240; -.
DR   KEGG; pls:VT03_15240; -.
DR   PATRIC; fig|1632864.3.peg.3475; -.
DR   OrthoDB; 226102at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000076318; 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; 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   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; 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:UP000076318};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          153..520
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          631..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        363
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   654 AA;  73893 MW;  1C5B6E02A24D7B5C CRC64;
     MSWQIWSDFD SHLWAEGTHM RAYEKLGAHP ETVDGQPSCR FAVWAPNASN VSVIGDFNGW
     QPGRDELQPV LGSGVWQGLL PRVRTGALYK FHIVSRHGDF RVDKADPFAF QAELPPGTAS
     RVCETGQFEW HDAEWRQSRG LRQAPTAPIS IYEVHLGSWR RGPQGETLTY RQLAPLLADY
     IHEMGFTHVE LMPLGEHPFG GSWGYQTIGY FAPTSRYGAP DDLRTLIDLL HQRGIGVLLD
     WVPAHFPRDE HGLAYFDGTH LFEASDPQRR SQPDWNTFIF DYGKPEVVSF LTSSALFWLD
     QFHIDGLRVD AVASMLYLDY SREPGEWTPN RQGGRENLEA IEFLRHLNRQ VSQHHPGTLV
     IAEESTAFSG VSRSVEQGGL GFSYKWDMGW MHDTLRYAAV QPAARREHHS ELTFRMNYAF
     SERFVLPLSH DEVVYGKGSL LSRMPGDDWQ KRAHLRLLFG YLFTQPGKKL LFMGGELGQW
     DEWNHDATVC WELLNSPEHR GLQRWVRDLN TFYRGQTALH ALDTEPGGFE WIEAHDAARS
     IIGYLRRPSH GDPLLVLLNW TAATVRNYRI GVPTGGDWTE LLNSDAALYG GSGQGNLGTV
     HAAPVPAQGR PYLLSVTVPP LALTIFRPTG ERPWGPSGFR SDPPSEPSVP RHES
//
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