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Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene

ganB

Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the beta-1,4-galactan linkages of arabinogalactan type I, a pectic substance found in plants such as soybeans.

Catalytic activityi

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei190Proton donorCurated1
Binding sitei263Substrate1
Active sitei288NucleophileCurated1
Binding sitei292Substrate1
Metal bindingi299Calcium1
Metal bindingi301Calcium1
Metal bindingi303Calcium1
Binding sitei307Substrate1
Binding sitei384Substrate1
Metal bindingi392Calcium1
Metal bindingi395Calcium1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.89. 669.

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinogalactan endo-beta-1,4-galactanase (EC:3.2.1.89)
Alternative name(s):
Endo-1,4-beta-galactanase
Short name:
Galactanase
Gene namesi
Name:ganB
Synonyms:galA, yvfO
Ordered Locus Names:BLi04276, BL00263
OrganismiBacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Taxonomic identifieri279010 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000000606 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000037156227 – 424Arabinogalactan endo-beta-1,4-galactanaseAdd BLAST398

Interactioni

Protein-protein interaction databases

STRINGi279010.BLi04276.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 54Combined sources5
Helixi58 – 63Combined sources6
Beta strandi73 – 75Combined sources3
Helixi78 – 84Combined sources7
Beta strandi89 – 94Combined sources6
Helixi113 – 125Combined sources13
Beta strandi129 – 134Combined sources6
Beta strandi136 – 139Combined sources4
Beta strandi142 – 144Combined sources3
Helixi150 – 152Combined sources3
Helixi157 – 177Combined sources21
Beta strandi182 – 190Combined sources9
Helixi201 – 218Combined sources18
Beta strandi222 – 228Combined sources7
Helixi236 – 246Combined sources11
Beta strandi252 – 258Combined sources7
Turni260 – 262Combined sources3
Helixi266 – 280Combined sources15
Beta strandi283 – 289Combined sources7
Beta strandi298 – 301Combined sources4
Beta strandi304 – 306Combined sources3
Helixi318 – 333Combined sources16
Beta strandi339 – 345Combined sources7
Helixi355 – 357Combined sources3
Helixi358 – 368Combined sources11
Beta strandi371 – 373Combined sources3
Helixi375 – 377Combined sources3
Turni378 – 380Combined sources3
Turni382 – 384Combined sources3
Helixi385 – 388Combined sources4
Helixi395 – 397Combined sources3
Beta strandi398 – 400Combined sources3
Helixi408 – 411Combined sources4
Helixi412 – 418Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8LX-ray2.60A/B26-424[»]
1UR0X-ray2.50A/B26-424[»]
1UR4X-ray2.20A/B26-424[»]
2CCRX-ray2.30A/B26-424[»]
2GFTX-ray2.30A/B26-424[»]
2J74X-ray2.60A/B28-424[»]
ProteinModelPortaliQ65CX5.
SMRiQ65CX5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ65CX5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 145Substrate binding4
Regioni229 – 230Substrate binding2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 53 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3867. LUCA.
HOGENOMiHOG000118034.
KOiK01224.
OMAiRWWFDEI.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q65CX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNVLAVFVV LIFVLGAFGT SGPAEAARDS GTAKSGLYVE KVSGLRKDFI
60 70 80 90 100
KGVDVSSIIA LEESGVAFYN ESGKKQDIFK TLKEAGVNYV RVRIWNDPYD
110 120 130 140 150
ANGNGYGGGN NDLEKAIQIG KRATANGMKL LADFHYSDFW ADPAKQKAPK
160 170 180 190 200
AWANLNFEDK KTALYQYTKQ SLKAMKAAGI DIGMVQVGNE TNGGLAGETD
210 220 230 240 250
WAKMSQLFNA GSQAVRETDS NILVALHFTN PETSGRYAWI AETLHRHHVD
260 270 280 290 300
YDVFASSYYP FWHGTLKNLT SVLTSVADTY GKKVMVAETS YTYTAEDGDG
310 320 330 340 350
HGNTAPKNGQ TLNNPVTVQG QANAVRDVIQ AVSDVGEAGI GVFYWEPAWI
360 370 380 390 400
PVGPAHRLEK NKALWETYGS GWATSYAAEY DPEDAGKWFG GSAVDNQALF
410 420
DFKGRPLPSL HVFQYVDTGT PFKN
Length:424
Mass (Da):46,225
Last modified:October 25, 2004 - v1
Checksum:iE6CC3D0D1B80D166
GO

Sequence cautioni

The sequence AAU25711 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU43089.1.
CP000002 Genomic DNA. Translation: AAU25711.1. Different initiation.
RefSeqiWP_011201775.1. NC_006322.1.

Genome annotation databases

EnsemblBacteriaiAAU25711; AAU25711; BL00263.
AAU43089; AAU43089; BLi04276.
GeneIDi3029947.
KEGGibld:BLi04276.
bli:BL00263.
PATRICi18954382. VBIBacLic203714_4366.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU43089.1.
CP000002 Genomic DNA. Translation: AAU25711.1. Different initiation.
RefSeqiWP_011201775.1. NC_006322.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8LX-ray2.60A/B26-424[»]
1UR0X-ray2.50A/B26-424[»]
1UR4X-ray2.20A/B26-424[»]
2CCRX-ray2.30A/B26-424[»]
2GFTX-ray2.30A/B26-424[»]
2J74X-ray2.60A/B28-424[»]
ProteinModelPortaliQ65CX5.
SMRiQ65CX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BLi04276.

Protein family/group databases

CAZyiGH53. Glycoside Hydrolase Family 53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU25711; AAU25711; BL00263.
AAU43089; AAU43089; BLi04276.
GeneIDi3029947.
KEGGibld:BLi04276.
bli:BL00263.
PATRICi18954382. VBIBacLic203714_4366.

Phylogenomic databases

eggNOGiCOG3867. LUCA.
HOGENOMiHOG000118034.
KOiK01224.
OMAiRWWFDEI.

Enzyme and pathway databases

BRENDAi3.2.1.89. 669.

Miscellaneous databases

EvolutionaryTraceiQ65CX5.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGANA_BACLD
AccessioniPrimary (citable) accession number: Q65CX5
Secondary accession number(s): Q62NF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 25, 2004
Last modified: November 2, 2016
This is version 86 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.