Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P39118

- GLGB_BACSU

UniProt

P39118 - GLGB_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

1,4-alpha-glucan branching enzyme GlgB

Gene

glgB

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.

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: 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.
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

        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: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...
MobiDBi 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.
InParanoidi P39118.
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: October 29, 2014
This is version 117 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