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Protein

1,4-alpha-glucan branching enzyme GlgB

Gene

glgB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei309 – 3091NucleophileBy similarity
Active sitei352 – 3521Proton donorBy similarity

GO - Molecular functioni

  1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB-HAMAP
  2. cation binding Source: InterPro
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU30980-MONOMER.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-alpha-glucan branching enzyme GlgB (EC:2.4.1.18)
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Alpha-(1->4)-glucan branching enzyme
Glycogen branching enzyme
Short name:
BE
Gene namesi
Name:glgB
Ordered Locus Names:BSU30980
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU30980. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6276271,4-alpha-glucan branching enzyme GlgBPRO_0000188683Add
BLAST

Proteomic databases

PaxDbiP39118.

Expressioni

Inductioni

Expressed exclusively on media containing carbon sources that allow efficient sporulation.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU30980.

Structurei

3D structure databases

ProteinModelPortaliP39118.
SMRiP39118. Positions 18-621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000283037.
InParanoidiP39118.
KOiK00700.
OMAiEGHLYKY.
OrthoDBiEOG6JX7GT.
PhylomeDBiP39118.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPiMF_00685. GlgB.
InterProiIPR006048. A-amylase_b_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 2 hits.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR01515. branching_enzym. 1 hit.

Sequencei

Sequence statusi: Complete.

P39118-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAASPTAHD VYLFHEGSLF KSYQLFGSHY RELNGKSGYE FCVWAPHASE
60 70 80 90 100
VRVAGDFNSW SGEEHVMHRV NDNGIWTLFI PGIGEKERYK YEIVTNNGEI
110 120 130 140 150
RLKADPYAIY SEVRPNTASL TYDLEGYSWQ DQKWQKKQKA KTLYEKPVFI
160 170 180 190 200
YELHLGSWKK HSDGRHYSYK ELSQTLIPYI KKHGFTHIEL LPVYEHPYDR
210 220 230 240 250
SWGYQGTGYY SPTSRFGPPH DLMKFVDECH QQNIGVILDW VPGHFCKDAH
260 270 280 290 300
GLYMFDGEPL YEYKEERDRE NWLWGTANFD LGKPEVHSFL ISNALYWAEF
310 320 330 340 350
YHIDGFRVDA VANILYWPNQ DERHTNPYAV DFLKKLNQTM REAYPHVMMI
360 370 380 390 400
AEDSTEWPQV TGAVEEGGLG FHYKWNMGWM NDVLKYMETP PEERRHCHQL
410 420 430 440 450
ISFSLLYAFS EHFVLPFSHD EVVYGKKSLL NKMPGDYWQK FAQYRLLLGY
460 470 480 490 500
MTVHPGKKLI FMGSEFAQFD EWKDTEQLDW FLDSFPMHQK ASVFTQDLLR
510 520 530 540 550
FYQKSKILYE HDHRAQSFEW IDVHNDEQSI FSFIRYGQKH GEALVIICNF
560 570 580 590 600
TPVVYHQYDV GVPFFTQYIE VLNSDSETYG GSGQINKKPL SAKKGALHHK
610 620
PCYITMTIPP YGISILRAVK KRGEIKR
Length:627
Mass (Da):73,665
Last modified:January 31, 1995 - v1
Checksum:i64B0A5553B6767BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25795 Genomic DNA. Translation: CAA81040.1.
AF008220 Genomic DNA. Translation: AAC00214.1.
AL009126 Genomic DNA. Translation: CAB15076.1.
PIRiS40048.
RefSeqiNP_390976.1. NC_000964.3.
WP_004398803.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB15076; CAB15076; BSU30980.
GeneIDi937993.
KEGGibsu:BSU30980.
PATRICi18978102. VBIBacSub10457_3239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25795 Genomic DNA. Translation: CAA81040.1.
AF008220 Genomic DNA. Translation: AAC00214.1.
AL009126 Genomic DNA. Translation: CAB15076.1.
PIRiS40048.
RefSeqiNP_390976.1. NC_000964.3.
WP_004398803.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP39118.
SMRiP39118. Positions 18-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU30980.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP39118.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15076; CAB15076; BSU30980.
GeneIDi937993.
KEGGibsu:BSU30980.
PATRICi18978102. VBIBacSub10457_3239.

Organism-specific databases

GenoListiBSU30980. [Micado]

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000283037.
InParanoidiP39118.
KOiK00700.
OMAiEGHLYKY.
OrthoDBiEOG6JX7GT.
PhylomeDBiP39118.

Enzyme and pathway databases

UniPathwayiUPA00164.
BioCyciBSUB:BSU30980-MONOMER.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPiMF_00685. GlgB.
InterProiIPR006048. A-amylase_b_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 2 hits.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR01515. branching_enzym. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glycogen in Bacillus subtilis: molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation."
    Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.
    Mol. Microbiol. 11:203-218(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiGLGB_BACSU
AccessioniPrimary (citable) accession number: P39118
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1995
Last sequence update: January 31, 1995
Last modified: January 6, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.