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Q4UZL7 (GLGB2_XANC8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1,4-alpha-glucan branching enzyme GlgB 2
EC=2.4.1.18
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 2
Alpha-(1->4)-glucan branching enzyme 2
Glycogen branching enzyme 2
Short name=BE 2
Gene names
Name:glgB2
Ordered Locus Names:XC_0422
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position By similarity. HAMAP MF_00685

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. HAMAP MF_00685

Pathway

Glycan biosynthesis; glycogen biosynthesis. HAMAP MF_00685

Subunit structure

Monomer By similarity. HAMAP MF_00685

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7297291,4-alpha-glucan branching enzyme GlgB 2 HAMAP MF_00685
PRO_0000260715

Sites

Active site4081Nucleophile By similarity
Active site4611Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4UZL7 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: C3D7257138AD810B

FASTA72979,972
        10         20         30         40         50         60 
MAEGGGGSAV ALQDLQAIAA GLPGDAFAVL GPHVQADGRL RVRVLAPGAE ALGLIDGRGK 

        70         80         90        100        110        120 
LLARMQASPI DGVFEGELPA DAAYRLRIVW PDVVQEIEDP YAFAPQIDES ALLQIGAGDG 

       130        140        150        160        170        180 
QALRANLGAR HVQVGELPAV RFAVWAPHAQ RVAVVGDFNG WEPRRHPMRQ RSGGIWELVL 

       190        200        210        220        230        240 
PRVETGARYK YAIITADGRV LLKADPVARQ SELPPATASV VASADAFAWT DAEWMARRSA 

       250        260        270        280        290        300 
AAEPAPLSIY EVHAASWRRD GHDQPLDWVS LAAQLIPYVQ ELGFTHIELL PITEHPFGGS 

       310        320        330        340        350        360 
WGYQPLGLYA PTARHGSPDG FAQFVDACHR AGIGVILDWV SAHFPDDAHG LSQFDGSATY 

       370        380        390        400        410        420 
EHADPREGMH RDWNTLIYNY GRPEVTAYLL GSAMEWIAHY HLDGLRVDAV ASMLYRDYGR 

       430        440        450        460        470        480 
AEGEWVPNAH GGRENLEAVA FLRQLTGEIA SQFPGVLTIA EESTAWPGVT APISEGGLGF 

       490        500        510        520        530        540 
THKWNMGWMH DTLHYMQRDP AARAQHHSQL TFGLVYAFSE RFVLPLSHDE VVHGTGGLLG 

       550        560        570        580        590        600 
QMPGDDWRRF ANLRAYLALM WAHPGDKLLF MGAEFGQWAD WNHDRSLDWH LLDHAPHRGM 

       610        620        630        640        650        660 
QQLVRDLNRA LRRVPALYRG NHRADGFEWS VADDARNSVL AFIRHDPDGG APLLAVSNLT 

       670        680        690        700        710        720 
PQPHHDYRVG VPRAGGWREI LNTDSAHYGG SNLGNGGRLL TEPTGMHGHA QSLRLTLPPL 


ATIYLQAEK

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References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed: 15899963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8004.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000050 Genomic DNA. Translation: AAY47506.1.
RefSeqYP_241526.1. NC_007086.1.

3D structure databases

HSSPHSSP built from PDB template 1M7X based on UniProtKB P07762.
ProteinModelPortalQ4UZL7.
SMRQ4UZL7. Positions 126-729.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4UZL7.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3381998.
GenomeReviewsGene locus XC_0422 in contig CP000050_GR.
KEGGxcb:XC_0422.
PATRIC24062074. VBIXanCam24967_0448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHBG287139.
OMARMQASAI.
PhylomeDBQ4UZL7.
ProtClustDBPRK12568.

Enzyme and pathway databases

BioCycXCAM314565:XC_0422-MONOMER.

Family and domain databases

HAMAPMF_00685. GlgB.
[Tree]
InterProIPR006407. 1-4-A-glucan_branch_enz.
IPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
KOK00700.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF13. PTHR10357:SF13. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
TIGRFAMsTIGR01515. Branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB2_XANC8
AccessionPrimary (citable) accession number: Q4UZL7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2005
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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