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Database: UniProt
Entry: A0A415R4A4_9FIRM
LinkDB: A0A415R4A4_9FIRM
Original site: A0A415R4A4_9FIRM 
ID   A0A415R4A4_9FIRM        Unreviewed;       790 AA.
AC   A0A415R4A4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=DWZ54_10600 {ECO:0000313|EMBL:RHM53566.1};
OS   Mitsuokella sp. AF33-22.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Mitsuokella.
OX   NCBI_TaxID=2292047 {ECO:0000313|EMBL:RHM53566.1, ECO:0000313|Proteomes:UP000284511};
RN   [1] {ECO:0000313|EMBL:RHM53566.1, ECO:0000313|Proteomes:UP000284511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF33-22 {ECO:0000313|EMBL:RHM53566.1,
RC   ECO:0000313|Proteomes:UP000284511};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RHM53566.1}.
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DR   EMBL; QRQA01000017; RHM53566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A415R4A4; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000284511; 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:RHM53566.1};
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          651..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..748
FT                   /note="Polar 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   790 AA;  90740 MW;  2AE2F73585A9B871 CRC64;
     MKTSDLSEFD LYLFHQGTNY HAYEMLGAHF VEQDGRKGVR FAVWAPHAKS VSVVGDFNGW
     DTRINPMTKV HDGEVWQVFI EGVEEGAVYK YAIEPQWGGP RIMKADPYGF YAEKKPETAS
     RVYDLGHYTW HDADWIERKK GESSYGRPML TYEVHAGSWR RTADGEYLSY RDLADQLIDY
     VKKMNYTHIE FMPLCEHPFD GSWGYQITGY YAVTSRFGTP DDFRYLVDKA HENGIAIIMD
     WVPGHFCKDE QGLRHFDGQT LYESDNEQLA ENWEWGTTNF DYGRTEVQSF LISNAMFWFE
     EYHIDGLRID AVANMLYLNY GRKDGEWTPN KYGDTGNLEA MDFLKKLNEN IFKYHPQALM
     IAEESTAWPL ISKPVYMGGM GFNYKWNMGW MNDMLRYMSL DPIYRKWNHD KVTFSFMYAF
     SENFVLPLSH DEVVHGKCSL ISKMPGDYWQ KFAGLRTFFA YWIAHPGKKL LFMGGEFGQF
     IEWNYDDSLD WHLPQQYPMH KKMLEYSRAL NKFYCDHKAL WEVDFDWNGF QWIDCNDSEN
     SIVSFIRKAD DPSDYIVAIC NFTPEVRHGY RVGMPEKGAY LEVFNSDDEA FGGSGVKNEG
     EILTEDVKWH DRDQSVVLTI PPMATIYLRH KGQLEGKRSF DDAAAVKTEA IGHEEQDSAA
     GAEAAAVRKT TRRKSTAKKA EETTEAPKRR RGRPRMTDEE KAAAKAKREA AKAAKKAAEG
     ETEEKPKTRR KRTTAASSSA STTRKTTARK TTKSAKSTKS TKSTTAKKTT TRKKTAATKT
     ASKEAAAGEA
//
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