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P39118

- GLGB_BACSU

UniProt

P39118 - GLGB_BACSU

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Protein
1,4-alpha-glucan branching enzyme GlgB
Gene
glgB, BSU30980
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei309 – 3091Nucleophile By similarity
Active sitei352 – 3521Proton donor By 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
Complete GO annotation...

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: Chromosome

Organism-specific databases

GenoListiBSU30980. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6276271,4-alpha-glucan branching enzyme GlgBUniRule annotation
PRO_0000188683Add
BLAST

Proteomic databases

PaxDbiP39118.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi224308.BSU30980.

Structurei

3D structure databases

ProteinModelPortaliP39118.
SMRiP39118. Positions 18-621.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000283037.
KOiK00700.
OMAiGELSHAW.
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

MAAASPTAHD VYLFHEGSLF KSYQLFGSHY RELNGKSGYE FCVWAPHASE    50
VRVAGDFNSW SGEEHVMHRV NDNGIWTLFI PGIGEKERYK YEIVTNNGEI 100
RLKADPYAIY SEVRPNTASL TYDLEGYSWQ DQKWQKKQKA KTLYEKPVFI 150
YELHLGSWKK HSDGRHYSYK ELSQTLIPYI KKHGFTHIEL LPVYEHPYDR 200
SWGYQGTGYY SPTSRFGPPH DLMKFVDECH QQNIGVILDW VPGHFCKDAH 250
GLYMFDGEPL YEYKEERDRE NWLWGTANFD LGKPEVHSFL ISNALYWAEF 300
YHIDGFRVDA VANILYWPNQ DERHTNPYAV DFLKKLNQTM REAYPHVMMI 350
AEDSTEWPQV TGAVEEGGLG FHYKWNMGWM NDVLKYMETP PEERRHCHQL 400
ISFSLLYAFS EHFVLPFSHD EVVYGKKSLL NKMPGDYWQK FAQYRLLLGY 450
MTVHPGKKLI FMGSEFAQFD EWKDTEQLDW FLDSFPMHQK ASVFTQDLLR 500
FYQKSKILYE HDHRAQSFEW IDVHNDEQSI FSFIRYGQKH GEALVIICNF 550
TPVVYHQYDV GVPFFTQYIE VLNSDSETYG GSGQINKKPL SAKKGALHHK 600
PCYITMTIPP YGISILRAVK KRGEIKR 627
Length:627
Mass (Da):73,665
Last modified:February 1, 1995 - v1
Checksum:i64B0A5553B6767BA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z25795 Genomic DNA. Translation: CAA81040.1 .
AF008220 Genomic DNA. Translation: AAC00214.1 .
AL009126 Genomic DNA. Translation: CAB15076.1 .
PIRi S40048.
RefSeqi NP_390976.1. NC_000964.3.
WP_004398803.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P39118.
SMRi P39118. Positions 18-621.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224308.BSU30980.

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbi P39118.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15076 ; CAB15076 ; BSU30980 .
GeneIDi 937993.
KEGGi bsu:BSU30980.
PATRICi 18978102. VBIBacSub10457_3239.

Organism-specific databases

GenoListi BSU30980. [Micado ]

Phylogenomic databases

eggNOGi COG0296.
HOGENOMi HOG000283037.
KOi K00700.
OMAi GELSHAW.
OrthoDBi EOG6JX7GT.
PhylomeDBi P39118.

Enzyme and pathway databases

UniPathwayi UPA00164 .
BioCyci BSUB:BSU30980-MONOMER.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPi MF_00685. GlgB.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 2 hits.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view ]
PIRSFi PIRSF000463. GlgB. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsi TIGR01515. branching_enzym. 1 hit.
ProtoNeti Search...

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(1994) [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(1997) [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(1997) [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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 115 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

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