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A4XHL8 (A4XHL8_CALS8) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 42. 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
Ordered Locus Names:Csac_0784
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length645 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

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 site3181Nucleophile By similarity HAMAP MF_00685
Active site3651Proton donor By similarity HAMAP MF_00685

Sequences

Sequence LengthMass (Da)Tools
A4XHL8 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 7797E370E4844560

FASTA64576,254
        10         20         30         40         50         60 
MIKKVKSTIY LSDIKRFEAG EHFESYKFLG SRVVNYRGKV GTVFCVWAPN AKSVSVVGDF 

        70         80         90        100        110        120 
NNWCGKNHKM MRVHGSGFWW LFVEGLLEGE LYKYEIIGAD GKRVLKADPY AIYSEVRPNT 

       130        140        150        160        170        180 
ASIVKNIPDY EWHDHEWMEK RKVTPPYDKP INIYEVHLAS WKMKKDGTVE KAGEFYNYRE 

       190        200        210        220        230        240 
LAHMLVDYLK VMNYTHIELL PVLEHPLDMS WGYQPTGYFS VTSRYGCPED FMYFVDIMHQ 

       250        260        270        280        290        300 
NGIGVIVDWV PAHFCKDEHG LYRFDGTFLY EYEDELLREN YTWGTATFDF SKPQVQSFLI 

       310        320        330        340        350        360 
SSAMFWFDIY HIDGIRVDAV SHIIYMNNNQ KNRYGGHENI EGIEFIKKLN KAIFSKYPNI 

       370        380        390        400        410        420 
LMIAEESTAF PLVTYPTYDG GLGFNYKWNM GWMNDTLKYM QFYPDERKYH HNLLTFSIMY 

       430        440        450        460        470        480 
AFSENFILPF SHDEVVHGKK SLLDKMPGEY NQKFANLRLL YGYMYTHPGK KLLFMGSEFG 

       490        500        510        520        530        540 
QFIEWRFYAS LDWLLLDYPM HRMLQHYVKS LNRFYLENKA LWELDHKMDG FRWIDVHNWE 

       550        560        570        580        590        600 
QSVISYLRFS KDPDDFLVVI CNFGLASYEN YKIGVPRKGI YMEVFNSDKA EFGGNNIVNT 

       610        620        630        640 
EKLKTIDEVW HGYPQCIEFR LPSLSCLIFK PVELFEDTKE KATDE 

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References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP66403.1.
RefSeqYP_001179594.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XHL8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4XHL8.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5087657.
GenomeReviewsGene locus Csac_0784 in contig CP000679_GR.
KEGGcsc:Csac_0784.
PATRIC21251140. VBICalSac56748_0892.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHBG287139.
OMAWRARINT.
ProtClustDBCLSK2472773.

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.
[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. 1 hit.
KOK00700.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF13. PTHR10357:SF13. 1 hit.
PfamPF00128. Alpha-amylase. 2 hits.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR01515. Branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA4XHL8_CALS8
AccessionPrimary (citable) accession number: A4XHL8
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)