ID E3CYX2_9BACT Unreviewed; 637 AA.
AC E3CYX2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=Apau_2156 {ECO:0000313|EMBL:EFQ24567.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ24567.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ24567.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ24567.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
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; CM001022; EFQ24567.1; -; Genomic_DNA.
DR RefSeq; WP_006301808.1; NZ_CM001022.1.
DR AlphaFoldDB; E3CYX2; -.
DR STRING; 584708.Apau_2156; -.
DR PaxDb; 584708-Apau_2156; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_0; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000005096; 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 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:UP000005096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 159..524
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 371
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 637 AA; 71886 MW; BC8EC0C0CB43DE4A CRC64;
MAGSVVHGVS LLTDYDLYLF REGNHTRLYE VLGAHPMTVE GVPGTLFSVW APNAEWVSVV
GDFNGWDDGA HRLASRWDGS GIHEGFVPGV GPGALYKYRL RSQVQGRLFE KGDPFAVSWE
APPKSASRVW SLDYDWGDGA WMASRGERNA LGAPWSVYEV HPGSWQRVPE EGNRFLGYRE
LGARLGNYVQ EMGFTHVEFL PVMEHPFYGS WGYQTLGYFA PTRRYGDPQD FMALVEELHR
RGIGVILDWV PSHFPQDGHG LAFFDGTCLY EHADPRQGFH PDWKSGVFNY GRNEVRSFLA
SSASFWLDRY HADGLRVDAV ASMLYLDYSR KEGQWVPNRY GGRENLEAVK FLQDANGELY
GRYEGIQTIA EESTAWPQVS RPVFLGGLGF GMKWNMGWMH DVLAHMGRDP IHRRWHWNEL
TFGMWYAYTE NFLLPLSHDE VVHGKGSLWG KMWGDSWNKA AGLRLLYGWM FAHPGKKLLF
MGDEFGQEGE WDHDRSLDWH ILTDPLHDGV RRWVRDLNAL LRSRPALHRL DFSPQGFQWI
DCTDSAGGVL ACLRLDGDGG TVLGVGNFTP VPRRGYRVGV PRGGFWRELL NSDAPCYGGS
GGGNLGGRQG EDVPCHGRPH SLCLDLPGLS FSFFEPA
//
