GLGB2_XANC8
ID GLGB2_XANC8 Reviewed; 729 AA.
AC Q4UZL7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB2 {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=XC_0422;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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; CP000050; AAY47506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4UZL7; -.
DR SMR; Q4UZL7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAY47506; AAY47506; XC_0422.
DR KEGG; xcb:XC_0422; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; IGGFWEL; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000420; 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..729
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000260715"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 729 AA; 79972 MW; C3D7257138AD810B CRC64;
MAEGGGGSAV ALQDLQAIAA GLPGDAFAVL GPHVQADGRL RVRVLAPGAE ALGLIDGRGK
LLARMQASPI DGVFEGELPA DAAYRLRIVW PDVVQEIEDP YAFAPQIDES ALLQIGAGDG
QALRANLGAR HVQVGELPAV RFAVWAPHAQ RVAVVGDFNG WEPRRHPMRQ RSGGIWELVL
PRVETGARYK YAIITADGRV LLKADPVARQ SELPPATASV VASADAFAWT DAEWMARRSA
AAEPAPLSIY EVHAASWRRD GHDQPLDWVS LAAQLIPYVQ ELGFTHIELL PITEHPFGGS
WGYQPLGLYA PTARHGSPDG FAQFVDACHR AGIGVILDWV SAHFPDDAHG LSQFDGSATY
EHADPREGMH RDWNTLIYNY GRPEVTAYLL GSAMEWIAHY HLDGLRVDAV ASMLYRDYGR
AEGEWVPNAH GGRENLEAVA FLRQLTGEIA SQFPGVLTIA EESTAWPGVT APISEGGLGF
THKWNMGWMH DTLHYMQRDP AARAQHHSQL TFGLVYAFSE RFVLPLSHDE VVHGTGGLLG
QMPGDDWRRF ANLRAYLALM WAHPGDKLLF MGAEFGQWAD WNHDRSLDWH LLDHAPHRGM
QQLVRDLNRA LRRVPALYRG NHRADGFEWS VADDARNSVL AFIRHDPDGG APLLAVSNLT
PQPHHDYRVG VPRAGGWREI LNTDSAHYGG SNLGNGGRLL TEPTGMHGHA QSLRLTLPPL
ATIYLQAEK
