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GLGB_NITHX
ID   GLGB_NITHX              Reviewed;         716 AA.
AC   Q1QNB1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=Nham_1464;
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR   EMBL; CP000319; ABE62286.1; -; Genomic_DNA.
DR   RefSeq; WP_011509977.1; NC_007964.1.
DR   AlphaFoldDB; Q1QNB1; -.
DR   SMR; Q1QNB1; -.
DR   STRING; 323097.Nham_1464; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABE62286; ABE62286; Nham_1464.
DR   KEGG; nha:Nham_1464; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_5; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 227746at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001953; 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; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.1180; -; 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   PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..716
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260669"
FT   ACT_SITE        398
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   716 AA;  80882 MW;  D8523F4B6EDE1D6C CRC64;
     MIELSSEARA IVEGRHSDPF HYLGRHREND RQVVRAYLPE ASDVRVVDEH GGETTLTRIH
     DAGLFLGDLP NGAKRYRLRA RFGADTVELE DPYRFPPILS DFDLYLLGEG TDQRLYDKLG
     AHPITMDGVG GTGFVVLAPN ARAVAVVGDF NCWDRRRHPM RVRGNGYWEL FIPGAQTGDR
     YKFAITDKSG SLLPLKSDPM AFAAEVRPNT ASIVVDEAAL PCPTPAAATI NARRAPISIY
     EVHLGSWRRG DDNRWLSYRE LADTLPRYAS SLGFTHIELM PVNEHPFDGS WGYQPTGLYA
     PTSRFGSPDD FAHLVDACHR EGLGVLLDWV PGHFPDDPHG LGHFDGTAFY EHANPLQGRH
     LDWDTLIYNY GRTEVVNFLV ANALFWLDRY GLDGLRVDAV ASMLYLDYSR AEGGWIPNKH
     GGRENLEAIA FLRRFNREVF AKFPHATTIA EESTAWPQVS RPIEFGGLGF GYKWNMGWMH
     DTLDYIGKDP IYRKHHHGQI LFGLHYAFSE NFILPLSHDE VVHEKRSILG RMPGDDWQRF
     ANLRAYYAFM FGHPGKKLMF MGAEFGQERE WNHDHALDWH LLDQARHQGV QAVVRDLNAL
     YRDVPALHEL DCDPAGFEWI MANDADRSVF AWMRKGESGR ARCLVIANFT PTVHRSYRVR
     VPFAGKWREA LNTDSAHYGG SNVGNNGVVE TLDGVIPELS LTLPPLAVIF LVPERA
 
 
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