ID H3NEK9_9LACT Unreviewed; 648 AA.
AC H3NEK9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=HMPREF9703_00990 {ECO:0000313|EMBL:EHR32874.1};
OS Dolosigranulum pigrum ATCC 51524.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Dolosigranulum.
OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR32874.1, ECO:0000313|Proteomes:UP000003599};
RN [1] {ECO:0000313|EMBL:EHR32874.1, ECO:0000313|Proteomes:UP000003599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR32874.1,
RC ECO:0000313|Proteomes:UP000003599};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL Submitted (JAN-2012) 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.
CC {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-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:EHR32874.1}.
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DR EMBL; AGEF01000009; EHR32874.1; -; Genomic_DNA.
DR RefSeq; WP_004636092.1; NZ_JH601103.1.
DR AlphaFoldDB; H3NEK9; -.
DR STRING; 29394.BWX42_03360; -.
DR PATRIC; fig|883103.3.peg.968; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_9; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000003599; 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; 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; 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:UP000003599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 155..501
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 312
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 648 AA; 75945 MW; 43FA2A7A080415B8 CRC64;
MYDERVIDEQ LKKDAYLFNS GQHFRCYHAL GCHRETREDV KGFRLTTWAP NAQHVSVVSD
FTDWESGQAL KLIENTGFWT GFFPTAQEND CYKFKITQAD GTVKLKSDPF AFAYEVRPKD
ASVVKVLPEK TWSDNIWMAN RKRLKIYERP LNIYEVHLSS WKHHEDGSWY SLKDLQAELI
PYVKEMGYTH IEFMPVMEHP LDRSWGYQIT GFFGFSSKYG TMEDFQDFVE ACHQQNIGVL
VDWVPSHFNR NDYAMAYFDG TPQFEYADPD RANNNRWGTL NFDLGKPQVH SFLISNALFW
LDIFHLDGIR VDAVSNMLYL DYDDGPWTPN EDGTNENRQG VAFIQKMNRV IFNEYSDVLM
MAEESTAYPG VTAPVHEGGL GFNYKWNMGW MNDTLKFFEM DPEFRKYHLE LITFSFMYVF
NENFILPFSH DEVVHGKKSL MHKMFGDRYN QFAGLRTIET FRMTHPGKNL HFMGAEYGQF
LEWDAEDQLD WLNLTDPVNI KHKHFMKTLN TLYRNHRSLW EIDHSWDGLV VLEADDRKHA
TLSYIRQGKN PRDFLVIVCN FKPHEHQQYR VGVPYEGIYE VILNTEMAEF GGKWSVPQPP
MKTLNKEANN QPYSIDVILP ALSVLIIRPK RIKGVNKRSI NKKGGRKD
//
