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B9MPC3 (B9MPC3_ANATD) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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:Athe_0558
OrganismAnaerocellum thermophilum (strain DSM 6725 / Z-1320) [Complete proteome] [HAMAP]
Taxonomic identifier521460 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length650 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
B9MPC3 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 4C7F300C10C8B603

FASTA65076,859
        10         20         30         40         50         60 
MIKKVKSTIY LSDIKKFESG EHFESYKFLG SKVVNYRGKV GTVFCVWAPN AKSVSVVGNF 

        70         80         90        100        110        120 
NNWRGENHKM MRVYGSGFWW LFVEGIGEGE LYKYEIIGAD GKRVLKADPY AIYSEKRPNT 

       130        140        150        160        170        180 
ASIVKNIPDY EWHDQEWMEK RKTTPPYDKP INIYEVHLAS WKMKKDGSIE KAGEFYNYRE 

       190        200        210        220        230        240 
LAHMLVDYIK EMNYNYIELL PVLEHPLDMS WGYQPTGYFS LTSRYGSIED FMYFVDYMHQ 

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

       310        320        330        340        350        360 
SSAMFWFDVY HIDGIRVDAV SHIIYMNNNQ KNRYGGHENI EGIEFIKKLN KAIFSKYPNV 

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

       430        440        450        460        470        480 
AFSENFILPF SHDEVVHGKK SLLDKMPGDY NQKFANLRLL YGYMYTHPGK KLLFMGGEFG 

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

       550        560        570        580        590        600 
QSVISYLRIS KEPDDYLVVI CNFSLASYEN YKIGVPKKGI YLEVFNSDKA EFGGNNIVNT 

       610        620        630        640        650 
EKLKTIDEVW HGYNQCIEFR LPALSCLIFK PIEFFNAQEE KNQNDNNIQI 

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References

[1]"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001393 Genomic DNA. Translation: ACM59684.1.
RefSeqYP_002572457.1. NC_012034.1.

3D structure databases

ProteinModelPortalB9MPC3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB9MPC3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7408684.
GenomeReviewsGene locus Athe_0558 in contig CP001393_GR.
KEGGate:Athe_0558.
PATRIC20898136. VBIAnaThe135187_0591.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARVYHQNG.
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 nameB9MPC3_ANATD
AccessionPrimary (citable) accession number: B9MPC3
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: December 14, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)