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A0L7G0 (A0L7G0_MAGSM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 44. 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 1 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 1 HAMAP MF_00685
Alpha-(1->4)-glucan branching enzyme 1 HAMAP MF_00685
Glycogen branching enzyme 1 HAMAP MF_00685
Gene names
Name:glgB1 HAMAP MF_00685
Ordered Locus Names:Mmc1_1392
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaMagnetococcus

Protein attributes

Sequence length723 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 site4031Nucleophile By similarity HAMAP MF_00685
Active site4541Proton donor By similarity HAMAP MF_00685

Sequences

Sequence LengthMass (Da)Tools
A0L7G0 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 4183D48D1D0EDE40

FASTA72383,275
        10         20         30         40         50         60 
MNLDPQQIQE LQSGFSADPF AVLGRHDQPD GQVAVTVLSP RTERLFLTNI GQEMTRIPDS 

        70         80         90        100        110        120 
DLFHWCGDGR ALPYHYRLRR VDAHGSQTEF HDPYSMPPMI GDLDRHLFNE GTHHHAGQFL 

       130        140        150        160        170        180 
GAHRMEVEGI RGVCFAVWAP NAQRVSVVGD FNQWDGRIHP MRLHQDSGIW EIFIPALKRG 

       190        200        210        220        230        240 
EHYKYEIRTT NGALLLKSDP YGHAHQLRPE NASIITEPSN YPWHDEVWMR ARSRFNWQKK 

       250        260        270        280        290        300 
PISIYEVHLG SWLDAATDPF PNYRELGKRL ARYCSEMGFT HVELMPINEH PFDGSWGYQS 

       310        320        330        340        350        360 
TGYFAVTSRF GDGDDFRAMV DQLHGANIGV ILDWVPAHFP KDAHGLGQFD GTALYEHQDP 

       370        380        390        400        410        420 
RLGEHQDWDT LIFNFGRLEV KSFLISSALH MLTRYHLDGL RVDAVASMLY LDYSREDWLP 

       430        440        450        460        470        480 
NKYGGRENLE AITFLRELNQ AVHHDCPGVL MIAEESTAWP QVTRPPELGG LGFNMKWNMG 

       490        500        510        520        530        540 
WMNDTLSYFS KDPIHRKYHH DNLTFSLYYA FSENFTLPFS HDEVVHGKAS MLGKMPGDEW 

       550        560        570        580        590        600 
QRFANLRLLY TYMFTHPGKK LLFMGCEFGQ SQEWNFSQAL PWELLEHTFH KGLQQLVKDL 

       610        620        630        640        650        660 
NLLYCKETAL HERDFTPDGF QWIDCHDSDQ SIISFQRKSS EGEVVVLLNF TPIPRDNYRI 

       670        680        690        700        710        720 
GVPRPGLYKE IFNADSGHYG GSNYGNGMSQ LLTEPYPWMN QLQSLVLNVP PMAGIILRCE 


QEG 

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References

[1]"Complete sequence of Magnetococcus sp. MC-1."
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., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK43903.1.
RefSeqYP_865309.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0L7G0.
SMRA0L7G0. Positions 112-722.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0L7G0.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4481811.
GenomeReviewsGene locus Mmc1_1392 in contig CP000471_GR.
KEGGmgm:Mmc1_1392.
NMPDRfig|156889.1.peg.2075.
PATRIC22429353. VBIMagSp23654_1433.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHBG287139.
OMARVYHQNG.
PhylomeDBA0L7G0.
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. 1 hit.
TIGRFAMsTIGR01515. Branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA0L7G0_MAGSM
AccessionPrimary (citable) accession number: A0L7G0
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)