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Q65CX5

- GANA_BACLD

UniProt

Q65CX5 - GANA_BACLD

Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene

ganB

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      Previous versions | rss
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    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

    Binds 1 calcium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei190 – 1901Proton donorCurated
    Binding sitei263 – 2631Substrate
    Active sitei288 – 2881NucleophileCurated
    Binding sitei292 – 2921Substrate
    Metal bindingi299 – 2991Calcium
    Metal bindingi301 – 3011Calcium
    Metal bindingi303 – 3031Calcium
    Binding sitei307 – 3071Substrate
    Binding sitei384 – 3841Substrate
    Metal bindingi392 – 3921Calcium
    Metal bindingi395 – 3951Calcium

    GO - Molecular functioni

    1. arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB-EC
    2. glucosidase activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciBLIC279010:GJ2P-4230-MONOMER.

    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 DSM 13 / ATCC 14580)
    Taxonomic identifieri279010 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000000606: Chromosome, UP000000608: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 424398Arabinogalactan endo-beta-1,4-galactanasePRO_0000371562Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi279010.BL00263.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 545
    Helixi58 – 636
    Beta strandi73 – 753
    Helixi78 – 847
    Beta strandi89 – 946
    Helixi113 – 12513
    Beta strandi129 – 1346
    Beta strandi136 – 1394
    Beta strandi142 – 1443
    Helixi150 – 1523
    Helixi157 – 17721
    Beta strandi182 – 1909
    Helixi201 – 21818
    Beta strandi222 – 2287
    Helixi236 – 24611
    Beta strandi252 – 2587
    Turni260 – 2623
    Helixi266 – 28015
    Beta strandi283 – 2897
    Beta strandi298 – 3014
    Beta strandi304 – 3063
    Helixi318 – 33316
    Beta strandi339 – 3457
    Helixi355 – 3573
    Helixi358 – 36811
    Beta strandi371 – 3733
    Helixi375 – 3773
    Turni378 – 3803
    Turni382 – 3843
    Helixi385 – 3884
    Helixi395 – 3973
    Beta strandi398 – 4003
    Helixi408 – 4114
    Helixi412 – 4187

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 36-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ65CX5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 1454Substrate binding
    Regioni229 – 2302Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 53 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3867.
    HOGENOMiHOG000118034.
    KOiK01224.
    OMAiIRLRLWV.
    OrthoDBiEOG6H4K5M.

    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

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    MKNVLAVFVV LIFVLGAFGT SGPAEAARDS GTAKSGLYVE KVSGLRKDFI    50
    KGVDVSSIIA LEESGVAFYN ESGKKQDIFK TLKEAGVNYV RVRIWNDPYD 100
    ANGNGYGGGN NDLEKAIQIG KRATANGMKL LADFHYSDFW ADPAKQKAPK 150
    AWANLNFEDK KTALYQYTKQ SLKAMKAAGI DIGMVQVGNE TNGGLAGETD 200
    WAKMSQLFNA GSQAVRETDS NILVALHFTN PETSGRYAWI AETLHRHHVD 250
    YDVFASSYYP FWHGTLKNLT SVLTSVADTY GKKVMVAETS YTYTAEDGDG 300
    HGNTAPKNGQ TLNNPVTVQG QANAVRDVIQ AVSDVGEAGI GVFYWEPAWI 350
    PVGPAHRLEK NKALWETYGS GWATSYAAEY DPEDAGKWFG GSAVDNQALF 400
    DFKGRPLPSL HVFQYVDTGT PFKN 424
    Length:424
    Mass (Da):46,225
    Last modified:October 25, 2004 - v1
    Checksum:iE6CC3D0D1B80D166
    GO

    Sequence cautioni

    The sequence AAU25711.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU43089.1.
    CP000002 Genomic DNA. Translation: AAU25711.1. Different initiation.
    RefSeqiWP_011198463.1. NC_006270.3.
    YP_006715543.1. NC_006322.1.
    YP_081349.1. NC_006270.3.

    Genome annotation databases

    EnsemblBacteriaiAAU25711; AAU25711; BL00263.
    AAU43089; AAU43089; BLi04276.
    GeneIDi3029947.
    3101427.
    KEGGibld:BLi04276.
    bli:BL00263.
    PATRICi18954382. VBIBacLic203714_4366.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017333 Genomic DNA. Translation: AAU43089.1 .
    CP000002 Genomic DNA. Translation: AAU25711.1 . Different initiation.
    RefSeqi WP_011198463.1. NC_006270.3.
    YP_006715543.1. NC_006322.1.
    YP_081349.1. NC_006270.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R8L X-ray 2.60 A/B 26-424 [» ]
    1UR0 X-ray 2.50 A/B 26-424 [» ]
    1UR4 X-ray 2.20 A/B 26-424 [» ]
    2CCR X-ray 2.30 A/B 26-424 [» ]
    2GFT X-ray 2.30 A/B 26-424 [» ]
    2J74 X-ray 2.60 A/B 28-424 [» ]
    ProteinModelPortali Q65CX5.
    SMRi Q65CX5. Positions 36-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279010.BL00263.

    Protein family/group databases

    CAZyi GH53. Glycoside Hydrolase Family 53.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU25711 ; AAU25711 ; BL00263 .
    AAU43089 ; AAU43089 ; BLi04276 .
    GeneIDi 3029947.
    3101427.
    KEGGi bld:BLi04276.
    bli:BL00263.
    PATRICi 18954382. VBIBacLic203714_4366.

    Phylogenomic databases

    eggNOGi COG3867.
    HOGENOMi HOG000118034.
    KOi K01224.
    OMAi IRLRLWV.
    OrthoDBi EOG6H4K5M.

    Enzyme and pathway databases

    BioCyci BLIC279010:GJ2P-4230-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q65CX5.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR011683. Glyco_hydro_53.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF07745. Glyco_hydro_53. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
      Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
      J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13 / ATCC 14580.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13 / ATCC 14580.
    3. "The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products."
      Ryttersgaard C., Le Nours J., Lo Leggio L., Joergensen C.T., Christensen L.L., Bjoernvad M., Larsen S.
      J. Mol. Biol. 341:107-117(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-424 IN COMPLEX WITH CALCIUM IONS AND SUBSTRATE ANALOGS, COFACTOR.

    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: October 1, 2014
    This is version 68 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

    External Data

    Dasty 3