ID R4PLT9_9BACT Unreviewed; 592 AA.
AC R4PLT9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=L336_0078 {ECO:0000313|EMBL:AGL61789.1};
OS Candidatus Saccharimonas aalborgensis.
OC Bacteria; Candidatus Saccharibacteria; Candidatus Saccharimonadia;
OC Candidatus Saccharimonadales; Candidatus Saccharimonadaceae; Saccharimonas.
OX NCBI_TaxID=1332188 {ECO:0000313|EMBL:AGL61789.1, ECO:0000313|Proteomes:UP000013893};
RN [1] {ECO:0000313|EMBL:AGL61789.1, ECO:0000313|Proteomes:UP000013893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM71 {ECO:0000313|EMBL:AGL61789.1};
RX PubMed=23707974; DOI=10.1038/nbt.2579;
RA Albertsen M., Hugenholtz P., Skarshewski A., Nielsen K.L., Tyson G.W.,
RA Nielsen P.H.;
RT "Genome sequences of rare, uncultured bacteria obtained by differential
RT coverage binning of multiple metagenomes.";
RL Nat. Biotechnol. 31:533-538(2013).
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};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; CP005957; AGL61789.1; -; Genomic_DNA.
DR AlphaFoldDB; R4PLT9; -.
DR STRING; 1332188.L336_0078; -.
DR KEGG; saal:L336_0078; -.
DR PATRIC; fig|1332188.3.peg.78; -.
DR HOGENOM; CLU_004245_5_1_0; -.
DR OrthoDB; 9800174at2; -.
DR Proteomes; UP000013893; Chromosome.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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:InterPro.
DR CDD; cd11325; AmyAc_GTHase; 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 InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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 PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000313|EMBL:AGL61789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013893};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGL61789.1}.
FT DOMAIN 124..470
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 592 AA; 66781 MW; 62B660629298D9E8 CRC64;
MSHQIKKHLG AIVRHNGVEF RVWAPFAKNV KLLTPYLGVF DGSNTYDMLS ENDGYWSAFV
KDAEVGQNYK FLIDTGNELL TKNDPRGRAL TASDNGVSVV VGSDFDWGDD LFMPIPREQQ
IIYELHIGTF NRRDPATTGT FYDAIEKLDY LLDLGINMIE VMPVTSMAYS NGWGYNVTDV
FSIENAYGGR HGLMEFVKAC HMRGIGVIID VVYNHFMSGD LWRFDGWYEN DRGGIYFYND
WRGDTPWGAR PDYGRAEVRQ FLIDSIVMWF NEYRVDGLRL DSTAYMRNTL GYNDDPAHDV
DGAWSLMQDI TDVAHRIRPG SIVIAEDTSG NDYITKQRQD GGCGFDAQWG IPFPHAIRKM
LGLGTSWPVD LGEQLLRAYN GDVFQRVIFS DSHDTAANGS TRITSAISPE NPNSTRVRQD
TIIASAITLT SPGIPMLLQG QEFLQEGAFT DWQVLEWEKT EQFAGIVKAH QDIIDLRKNT
YGNTSGLLGQ SVRVFHRNDQ GQVFGYHRWS RGGPGDDVLV LINFGDTEYH EYHLGFPRPG
EWRIRFNSSW QGYNSDFPEL TPDSVSTDDS CNLAMDIPAR SVLILSQDAT AS
//
