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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)DescriptionActionsGraphical viewLength
Active sitei411Nucleophile1
Active sitei464Proton donor1

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

BioCyciMTBH37RV:G185E-5505-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001887181 – 7311,4-alpha-glucan branching enzyme GlgBAdd BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1731
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 24Combined sources9
Helixi30 – 33Combined sources4
Beta strandi34 – 48Combined sources15
Beta strandi57 – 59Combined sources3
Beta strandi72 – 75Combined sources4
Beta strandi87 – 91Combined sources5
Beta strandi98 – 100Combined sources3
Helixi103 – 105Combined sources3
Helixi112 – 119Combined sources8
Helixi126 – 128Combined sources3
Beta strandi130 – 138Combined sources9
Beta strandi140 – 152Combined sources13
Beta strandi157 – 163Combined sources7
Helixi164 – 166Combined sources3
Helixi179 – 181Combined sources3
Beta strandi183 – 189Combined sources7
Beta strandi196 – 202Combined sources7
Beta strandi208 – 211Combined sources4
Beta strandi217 – 219Combined sources3
Helixi239 – 245Combined sources7
Helixi250 – 252Combined sources3
Beta strandi256 – 260Combined sources5
Turni262 – 264Combined sources3
Helixi271 – 285Combined sources15
Beta strandi288 – 293Combined sources6
Helixi301 – 303Combined sources3
Beta strandi309 – 314Combined sources6
Helixi316 – 318Combined sources3
Helixi321 – 333Combined sources13
Beta strandi337 – 342Combined sources6
Turni351 – 358Combined sources8
Beta strandi370 – 372Combined sources3
Helixi386 – 402Combined sources17
Beta strandi407 – 410Combined sources4
Helixi414 – 417Combined sources4
Helixi439 – 455Combined sources17
Beta strandi460 – 463Combined sources4
Helixi476 – 478Combined sources3
Beta strandi484 – 487Combined sources4
Helixi489 – 500Combined sources12
Helixi503 – 509Combined sources7
Helixi510 – 514Combined sources5
Helixi515 – 518Combined sources4
Turni519 – 521Combined sources3
Beta strandi525 – 529Combined sources5
Helixi531 – 533Combined sources3
Helixi541 – 544Combined sources4
Helixi549 – 565Combined sources17
Beta strandi566 – 573Combined sources8
Helixi576 – 578Combined sources3
Turni586 – 588Combined sources3
Helixi592 – 596Combined sources5
Beta strandi597 – 600Combined sources4
Helixi601 – 617Combined sources17
Helixi619 – 621Combined sources3
Turni622 – 626Combined sources5
Helixi628 – 630Combined sources3
Beta strandi631 – 638Combined sources8
Turni639 – 642Combined sources4
Beta strandi643 – 649Combined sources7
Beta strandi655 – 661Combined sources7
Beta strandi663 – 665Combined sources3
Beta strandi667 – 676Combined sources10
Beta strandi678 – 685Combined sources8
Helixi689 – 691Combined sources3
Beta strandi701 – 706Combined sources6
Beta strandi712 – 720Combined sources9
Beta strandi724 – 730Combined sources7

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0296. LUCA.
KOiK00700.
OMAiHFPSDDF.
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. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K1DX-ray2.33A10-731[»]
ProteinModelPortaliP9WN45.
SMRiP9WN45.
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.
OMAiHFPSDDF.
PhylomeDBiP9WN45.

Enzyme and pathway databases

UniPathwayiUPA00164.
UPA00934.
BioCyciMTBH37RV:G185E-5505-MONOMER.

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. 1 hit.
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...

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: November 2, 2016
This is version 20 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.