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A1A165 (A1A165_BIFAA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP MF_00685

EC=2.4.1.18 HAMAP MF_00685
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase HAMAP MF_00685
Alpha-(1->4)-glucan branching enzyme HAMAP MF_00685
Glycogen branching enzyme HAMAP MF_00685
Gene names
Name:glgB HAMAP MF_00685 EMBL BAF39448.1
Ordered Locus Names:BAD_0667
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length751 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 SAAS SAAS006407

Pathway

Glycan biosynthesis; glycogen biosynthesis. HAMAP MF_00685 SAAS SAAS006407

Subunit structure

Monomer By similarity. HAMAP MF_00685

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily. HAMAP MF_00685

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site4321Nucleophile By similarity HAMAP MF_00685
Active site4851Proton donor By similarity HAMAP MF_00685

Sequences

Sequence LengthMass (Da)Tools
A1A165 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 5F02E4B328312A96

FASTA75184,570
        10         20         30         40         50         60 
MATESKIKED SVAVPVAQGD LDAVSNGTFY NPHEVLGGHL GPDEHEDVVT IRVLRPLAKS 

        70         80         90        100        110        120 
VTIITENART QAVHEHNGVF MALIPAIKTD DGFGVPDYRI STEYEDGSTV VSDDPYRYLP 

       130        140        150        160        170        180 
TIGDLDMYLF GEGRHERLWE ALGARVLRYD DPLGSNDGVK GEQLAGTAFT VWAPNAHAVR 

       190        200        210        220        230        240 
VVGDFNGWNG RTHAMRELGS SGVWELFIPG VGTGTIYKYE ILNANNEWVM KADPMERSHE 

       250        260        270        280        290        300 
IPPRTGSIVV DSVHAWHDEN WMDQRAKTDP HNGPVSIYEV HASSWRKDVK NYRELADKLV 

       310        320        330        340        350        360 
PYVQKEGFTH VEFMPLAEHP FSGSWGYQVT GYYAIDSRLG GPDDFKYLVE KMHEAGIGVI 

       370        380        390        400        410        420 
MDWVPAHFPK DAFALGRFDG TPLYEDPDPT RGEHPDWGTY VFNFGRREVR NFLVANACFW 

       430        440        450        460        470        480 
LDEYHIDALR VDAVSSMLYL DYSRKPGQWH PNIYGGRENL EAIDFLKEAT ATAYKNNPGI 

       490        500        510        520        530        540 
MMIAEESTAY PGITAPTDAG GLGFGLKWNM GWMHDTLQYL HEEPINRKWH HNEITFSMVY 

       550        560        570        580        590        600 
AYSEHYVLPI SHDEVVYGKG SLFGKMPGDD WQRYAGVRAL FAYQWAHPGK KLSFMGNEVA 

       610        620        630        640        650        660 
QYGEWDHDGS VDWDVLNWPD HRGVQKLVAD LNTLYKASPA LWSQDFDPAG FQWLTSDDAD 

       670        680        690        700        710        720 
HNTLSFVRIG KDGEQMVVVV NFSGEAWEDY QVPLTKGGKW TEVLTTDDKK YGGSDIHNGT 

       730        740        750 
FKAVKGEYHS RDWSAKITVP ALGAVFLKPE L 

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009256 Genomic DNA. Translation: BAF39448.1.
RefSeqYP_909530.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A165.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A165.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4557707.
GenomeReviewsGene locus BAD_0667 in contig AP009256_GR.
KEGGbad:BAD_0667.
NMPDRfig|1680.3.peg.1430.
PATRIC21100687. VBIBifAdo27973_0721.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHBG287139.
OMADGTCLYE.
ProtClustDBPRK05402.

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. 2 hits.
TIGRFAMsTIGR01515. Branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA1A165_BIFAA
AccessionPrimary (citable) accession number: A1A165
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)