GLGB2_XANAC
ID GLGB2_XANAC Reviewed; 719 AA.
AC Q8PQA2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 2;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2;
DE AltName: Full=Glycogen branching enzyme 2;
DE Short=BE 2;
GN Name=glgB2; OrderedLocusNames=XAC0426;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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:0000250}.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE008923; AAM35317.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8PQA2; -.
DR SMR; Q8PQA2; -.
DR STRING; 190486.XAC0426; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAM35317; AAM35317; XAC0426.
DR KEGG; xac:XAC0426; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; IGGFWEL; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000576; 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; Transferase.
FT CHAIN 1..719
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000188765"
FT ACT_SITE 398
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 451
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 719 AA; 79256 MW; 9E992FD6268E8E02 CRC64;
MSQTLQALAD GLPADAFAVL GPKLLADGRR QVRVLAPGAE AMGLIDPRGK LLARMQASAI
DGVFEGTLAV DGPYRLRIVW PDRVQEVEDP YAFAATLDES LLLQIAAGDG QALRRALGAQ
HLHCGDVPGV RFALWAPHAQ RVAVVGDFNG WDVRRHPMRQ RIGGFWELFL PRVDAGARYK
YAVTAADGRV LLKADPVARQ TELPPATASV VPSAATFAWT DAAWMANRDP AAVPGPLSIY
EVHAASWRRD GHNQPLDWPT LAEQLIPYVQ QLGFTHIELL PITEHPFGGS WGYQPLGLYA
PTARHGSPDG FAQFVDACHR AGIGVILDWV SAHFPDDAHG LAQFDGAALY EHADPREGMH
RDWNTLIYNY GRPEVTAYLL GSALEWIEHY HLDGLRVDAV ASMLYRDYGR AEGEWVPNAH
GGRENLEAVA FLRQLNRDIA TQFPGVLTIA EESTAWPGVT AAISDGGLGF THKWNMGWMH
DTLGYMQRDP AERAHHHSQL TFGLVYAFDE RFVLPLSHDE VVHGTGGLLG QMPGDDWRRF
ANLRAYLALM WAHPGDKLLF MGAEFGQWAD WNHDQSLDWH LLDGARHRGM QQLVGDLNAA
LRRTPALYRG THRAEGFDWS VADDARNSVL AFVRHDPDGG APLLAVSNLT PQPHHDYHVG
VPRAGLWREI LNTDSAHYGG SNLGNSGRLA TEPVGMHGHA QRLRLTLPPL ATIYLQAEK
