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Protein

1,4-alpha-glucan branching enzyme GlgB

Gene

glgB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential enzyme that catalyzes the formation of the alpha-1,6-glucosidic linkages in glucan chains 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. Is involved in the biosynthesis of both glycogen and capsular alpha-D-glucan.2 Publications

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.2 Publications

Enzyme regulationi

Is inhibited by divalent cations such as Zn2+ and Cu2+, but not by Mg2+, Mn2+ and Ca2+. Is not inhibited by several known inhibitors of the GH13 family such as ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose.2 Publications

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius. Loses 20% of its maximum activity at 37 degrees Celsius and is nearly inactive above 55 degrees Celsius.1 Publication

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

Pathwayi: capsule polysaccharide biosynthesis

This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei411 – 4111Nucleophile
Active sitei464 – 4641Proton donor

GO - Molecular functioni

GO - Biological processi

  • capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
  • glucan biosynthetic process Source: MTBBASE
  • glycogen biosynthetic process Source: MTBBASE
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Capsule biogenesis/degradation, Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

UniPathwayiUPA00164.
UPA00934.

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:Rv1326c
ORF Names:MTCY130.11c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1326c.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Disruption of glgB is lethal for the bacteria in vitro. Affects the production of both extracellular alpha-D-glucan and intracellular glycogen.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7317311,4-alpha-glucan branching enzyme GlgBPRO_0000188718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi193 ↔ 6172 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP9WN45.

Interactioni

Subunit structurei

Monomer. Interacts with WhiB1 via an intermolecular disulfide bond.2 Publications

Protein-protein interaction databases

STRINGi83332.Rv1326c.

Structurei

Secondary structure

1
731
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 249Combined sources
Helixi30 – 334Combined sources
Beta strandi34 – 4815Combined sources
Beta strandi57 – 593Combined sources
Beta strandi72 – 754Combined sources
Beta strandi87 – 915Combined sources
Beta strandi98 – 1003Combined sources
Helixi103 – 1053Combined sources
Helixi112 – 1198Combined sources
Helixi126 – 1283Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi140 – 15213Combined sources
Beta strandi157 – 1637Combined sources
Helixi164 – 1663Combined sources
Helixi179 – 1813Combined sources
Beta strandi183 – 1897Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi217 – 2193Combined sources
Helixi239 – 2457Combined sources
Helixi250 – 2523Combined sources
Beta strandi256 – 2605Combined sources
Turni262 – 2643Combined sources
Helixi271 – 28515Combined sources
Beta strandi288 – 2936Combined sources
Helixi301 – 3033Combined sources
Beta strandi309 – 3146Combined sources
Helixi316 – 3183Combined sources
Helixi321 – 33313Combined sources
Beta strandi337 – 3426Combined sources
Turni351 – 3588Combined sources
Beta strandi370 – 3723Combined sources
Helixi386 – 40217Combined sources
Beta strandi407 – 4104Combined sources
Helixi414 – 4174Combined sources
Helixi439 – 45517Combined sources
Beta strandi460 – 4634Combined sources
Helixi476 – 4783Combined sources
Beta strandi484 – 4874Combined sources
Helixi489 – 50012Combined sources
Helixi503 – 5097Combined sources
Helixi510 – 5145Combined sources
Helixi515 – 5184Combined sources
Turni519 – 5213Combined sources
Beta strandi525 – 5295Combined sources
Helixi531 – 5333Combined sources
Helixi541 – 5444Combined sources
Helixi549 – 56517Combined sources
Beta strandi566 – 5738Combined sources
Helixi576 – 5783Combined sources
Turni586 – 5883Combined sources
Helixi592 – 5965Combined sources
Beta strandi597 – 6004Combined sources
Helixi601 – 61717Combined sources
Helixi619 – 6213Combined sources
Turni622 – 6265Combined sources
Helixi628 – 6303Combined sources
Beta strandi631 – 6388Combined sources
Turni639 – 6424Combined sources
Beta strandi643 – 6497Combined sources
Beta strandi655 – 6617Combined sources
Beta strandi663 – 6653Combined sources
Beta strandi667 – 67610Combined sources
Beta strandi678 – 6858Combined sources
Helixi689 – 6913Combined sources
Beta strandi701 – 7066Combined sources
Beta strandi712 – 7209Combined sources
Beta strandi724 – 7307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K1DX-ray2.33A10-731[»]
ProteinModelPortaliP9WN45.
SMRiP9WN45. Positions 10-731.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0296. LUCA.
KOiK00700.
OMAiDATEVWV.
PhylomeDBiP9WN45.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPiMF_00685. GlgB.
InterProiIPR006048. A-amylase/branching_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
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. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsiTIGR01515. branching_enzym. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WN45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSEKLTGE HLAPEPAEMA RLVAGTHHNP HGILGAHEYD DHTVIRAFRP
60 70 80 90 100
HAVEVVALVG KDRFSLQHLD SGLFAVALPF VDLIDYRLQV TYEGCEPHTV
110 120 130 140 150
ADAYRFLPTL GEVDLHLFAE GRHERLWEVL GAHPRSFTTA DGVVSGVSFA
160 170 180 190 200
VWAPNAKGVS LIGEFNGWNG HEAPMRVLGP SGVWELFWPD FPCDGLYKFR
210 220 230 240 250
VHGADGVVTD RADPFAFGTE VPPQTASRVT SSDYTWGDDD WMAGRALRNP
260 270 280 290 300
VNEAMSTYEV HLGSWRPGLS YRQLARELTD YIVDQGFTHV ELLPVAEHPF
310 320 330 340 350
AGSWGYQVTS YYAPTSRFGT PDDFRALVDA LHQAGIGVIV DWVPAHFPKD
360 370 380 390 400
AWALGRFDGT PLYEHSDPKR GEQLDWGTYV FDFGRPEVRN FLVANALYWL
410 420 430 440 450
QEFHIDGLRV DAVASMLYLD YSRPEGGWTP NVHGGRENLE AVQFLQEMNA
460 470 480 490 500
TAHKVAPGIV TIAEESTPWS GVTRPTNIGG LGFSMKWNMG WMHDTLDYVS
510 520 530 540 550
RDPVYRSYHH HEMTFSMLYA FSENYVLPLS HDEVVHGKGT LWGRMPGNNH
560 570 580 590 600
VKAAGLRSLL AYQWAHPGKQ LLFMGQEFGQ RAEWSEQRGL DWFQLDENGF
610 620 630 640 650
SNGIQRLVRD INDIYRCHPA LWSLDTTPEG YSWIDANDSA NNVLSFMRYG
660 670 680 690 700
SDGSVLACVF NFAGAEHRDY RLGLPRAGRW REVLNTDATI YHGSGIGNLG
710 720 730
GVDATDDPWH GRPASAVLVL PPTSALWLTP A
Length:731
Mass (Da):81,729
Last modified:April 16, 2014 - v1
Checksum:iEE2BFEF765352617
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44084.1.
PIRiB70770.
RefSeqiNP_215842.1. NC_000962.3.
WP_003900318.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44084; CCP44084; Rv1326c.
GeneIDi886893.
KEGGimtu:Rv1326c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44084.1.
PIRiB70770.
RefSeqiNP_215842.1. NC_000962.3.
WP_003900318.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K1DX-ray2.33A10-731[»]
ProteinModelPortaliP9WN45.
SMRiP9WN45. Positions 10-731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1326c.

Proteomic databases

PaxDbiP9WN45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44084; CCP44084; Rv1326c.
GeneIDi886893.
KEGGimtu:Rv1326c.

Organism-specific databases

TubercuListiRv1326c.

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0296. LUCA.
KOiK00700.
OMAiDATEVWV.
PhylomeDBiP9WN45.

Enzyme and pathway databases

UniPathwayiUPA00164.
UPA00934.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPiMF_00685. GlgB.
InterProiIPR006048. A-amylase/branching_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
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. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsiTIGR01515. branching_enzym. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Expression and characterization of alpha-(1,4)-glucan branching enzyme Rv1326c of Mycobacterium tuberculosis H37Rv."
    Garg S.K., Alam M.S., Kishan K.V., Agrawal P.
    Protein Expr. Purif. 51:198-208(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISULFIDE BONDS.
    Strain: ATCC 25618 / H37Rv.
  3. "Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice."
    Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y., Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A., Daffe M., Jackson M.
    Mol. Microbiol. 70:762-774(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CAPSULAR GLUCAN AND GLYCOGEN BIOSYNTHESIS, DISRUPTION PHENOTYPE, ESSENTIALITY, PATHWAY.
    Strain: ATCC 25618 / H37Rv.
  4. "Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide."
    Garg S., Alam M.S., Bajpai R., Kishan K.R., Agrawal P.
    BMC Biochem. 10:1-1(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WHIB1, DISULFIDE BOND.
    Strain: ATCC 25618 / H37Rv.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  6. "Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity."
    Pal K., Kumar S., Sharma S., Garg S.K., Alam M.S., Xu H.E., Agrawal P., Swaminathan K.
    J. Biol. Chem. 285:20897-20903(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 10-371, CATALYTIC ACTIVITY, ENZYME REGULATION, CATALYTIC MECHANISM.
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiGLGB_MYCTU
AccessioniPrimary (citable) accession number: P9WN45
Secondary accession number(s): L0T925, Q10625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 11, 2016
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cysteine residues of GlgB form structural disulfide bond(s), which allow the protein to exist in two different redox-dependent conformational states. Although the conformational change do not affect the branching enzyme activity, the change in surface hydrophobicity could influence the interaction or dissociation of different cellular proteins with GlgB in response to different physiological states.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.