(data stored in ACNUC7421 zone)

HOGENOM: XAORY1_1_PE101

ID   XAORY1_1_PE101                       STANDARD;      PRT;   728 AA.
AC   XAORY1_1_PE101; Q5H6Q3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=1,4-alpha-glucan-branching enzyme 2; EC=2.4.1 18;AltName:
DE   Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
DE   2;AltName: Full=Glycogen-branching enzyme 2; Short=BE 2;
DE   (XAORY1_1.PE101).
GN   Name=glgB2; OrderedLocusNames=XOO0113;
OS   XANTHOMONAS ORYZAE PV. ORYZAE KACC10331.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS XAORY1_1.PE101.
CC       Xanthomonas oryzae pv. oryzae KACC10331 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:GLGB2_XANOR
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic
CC       linkages in glycogen by scission of a 1,4-alpha-linked
CC       oligosaccharide from growing alpha-1,4-glucan chains and the
CC       subsequent attachment of the oligosaccharide to the alpha-1,6
CC       position (By similarity).
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       chain to a primary hydroxy group in a similar glucan chain.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW73367.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000283037 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5H6Q3; -.
DR   EMBL; AE013598; AAW73367.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_198752.6; NC_006834.1.
DR   ProteinModelPortal; Q5H6Q3; -.
DR   SMR; Q5H6Q3; 115-720.
DR   GeneID; 3265719; -.
DR   GenomeReviews; AE013598_GR; XOO0113.
DR   KEGG; xoo:XOO0113; -.
DR   NMPDR; fig|291331.3.peg.430; -.
DR   OMA; RMQASAI; -.
DR   ProtClustDB; PRK12568; -.
DR   BioCyc; XORY291331:XOO0113-MON; -.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA: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-KW.
DR   HAMAP; MF_00685; GlgB; 1; -.
DR   InterPro; IPR006407; 1-4-A-glucan_branch_enz.
DR   InterPro; IPR006048; A-amylase_b_C.
DR   InterPro; IPR015902; Alpha_amylase.
DR   InterPro; IPR013780; Glyco_hydro_13_b.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013781; Glyco_hydro_subgr_catalytic.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   PANTHER; PTHR10357; Alpha_amylase; 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   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   TIGRFAMs; TIGR01515; Branching_enzym; 1.
DR   HOGENOMDNA; XAORY1_1.PE101; -.
KW   Complete proteome; Glycogen biosynthesis; Glycosyltransferase;
KW   Transferase.
SQ   SEQUENCE   728 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTEGISEMS QTLQALADGL PVDAFAVLGP HPLADGRRQV RVLAPGAEAM GLIDSRGKLL
     ARMQASAIDG VFEGILSIEG PYRLRIVWPD MVQEIEDPYA FAVTLDESLL LQIAAGDGQA
     LRRALGAQHV QCGEVPGVRF AVWAPHAQRV AVVGDFNGWD VRRHPMRQRI GGFWELFLPR
     VEAGPRYKYA VTAADGRVLL KADPVARQTE LPPATASVVP GTDTFAWTDA AWMAKRDPSA
     VPAPLSIYEV HAASWRRDGH NQPLDWPTLA EQLIPYVQQL RFTHIELLPI TEHPFGGSWG
     YQPLGLYAPT ARHGSPDGFA QFVDACHRAG IGVILDWVSA HFPDDAHGLA QFDGAALYEH
     ADPREGMHRD WNTLIYNYGR PEVTAYLLGS ALEWIDHYHL DGLRVDAVAS MLYRDYGRAE
     GEWVPNAHGG RENLEAVAFL RQLNREIAAH FPGVLTIAEE STAWPGVTAA ISDGGLGFTH
     KWNMGWMHDT LSYMQRDPAE RAHHHSQLTF GLVYAFDERF VLPISHDEVV HGTGGLLGQM
     PGDDWRRFAN LRAYLALMWA HPGDKLLFMG AEFGQWADWN HDQSLDWHLL EGARHRGVQL
     LVGDLNATLR RTPALYRGTH RAKGFDWSVA DDARNSVLAF IRHDPDGGGV PLLAVSNLTA
     QPLHDYGVGV PRAGAWREIL NTDSAHYGGS NLGNSGRLAT EPMGMHGHAQ RLRLTLPPLA
     TIYLQAEK
//

If you have problems or comments...

PBIL Back to PBIL home page