Skip Header

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

Beta-agarase A

Gene

agaA

Organism
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.1 Publication

Kineticsi

kcat is 150 sec(-1).

  1. KM=2 mM for agarose1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei73Substrate1 Publication1
    Binding sitei144Substrate1 Publication1
    Active sitei147Nucleophile1 Publication1
    Active sitei152Proton donor1 Publication1
    Binding sitei176Substrate1 Publication1
    Binding sitei271Substrate1 Publication1

    GO - Molecular functioni

    • beta-agarase activity Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: UniProtKB
    • metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.81. 7557.

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-agarase A (EC:3.2.1.81)
    Cleaved into the following chain:
    Gene namesi
    Name:agaA
    Ordered Locus Names:zobellia_4203
    OrganismiZobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
    Taxonomic identifieri63186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeZobellia
    Proteomesi
    • UP000008898 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi147E → S: Abolishes beta-agarase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 19Sequence analysisAdd BLAST19
    ChainiPRO_500005526820 – 539Beta-agarase AAdd BLAST520
    ChainiPRO_500005526920 – 295Beta-agarase A catalytic chainAdd BLAST276

    Post-translational modificationi

    Proteolytically cleaved into mature beta-agarase A catalytic chain (AgaAc).1 Publication

    Expressioni

    Inductioni

    When cells are grown with the low sulfated agar.1 Publication

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1539
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni22 – 25Combined sources4
    Beta strandi36 – 40Combined sources5
    Helixi42 – 44Combined sources3
    Beta strandi50 – 53Combined sources4
    Helixi59 – 62Combined sources4
    Beta strandi65 – 68Combined sources4
    Beta strandi70 – 72Combined sources3
    Beta strandi79 – 81Combined sources3
    Helixi83 – 85Combined sources3
    Beta strandi86 – 91Combined sources6
    Beta strandi93 – 101Combined sources9
    Beta strandi104 – 107Combined sources4
    Beta strandi109 – 114Combined sources6
    Beta strandi118 – 127Combined sources10
    Beta strandi130 – 140Combined sources11
    Beta strandi146 – 154Combined sources9
    Helixi157 – 159Combined sources3
    Helixi161 – 164Combined sources4
    Beta strandi166 – 175Combined sources10
    Turni176 – 179Combined sources4
    Beta strandi180 – 182Combined sources3
    Helixi187 – 189Combined sources3
    Beta strandi190 – 192Combined sources3
    Helixi198 – 200Combined sources3
    Beta strandi203 – 211Combined sources9
    Beta strandi214 – 219Combined sources6
    Beta strandi222 – 227Combined sources6
    Helixi229 – 232Combined sources4
    Turni237 – 240Combined sources4
    Beta strandi247 – 254Combined sources8
    Turni257 – 259Combined sources3
    Helixi265 – 269Combined sources5
    Turni271 – 273Combined sources3
    Beta strandi274 – 288Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O4YX-ray1.48A20-295[»]
    1URXX-ray1.70A20-290[»]
    SMRiG0L322.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini21 – 289GH16PROSITE-ProRule annotationAdd BLAST269

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni82 – 92Substrate binding1 PublicationAdd BLAST11
    Regioni96 – 98Substrate binding1 Publication3

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 16 family.Curated
    Contains 1 GH16 (glycosyl hydrolase family 16) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK01219.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR008979. Galactose-bd-like.
    IPR000757. GH16.
    IPR026444. Secre_tail.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.
    PROSITEiPS51762. GH16_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    G0L322-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKNYLLLYF IFLLCGSIAA QDWNGIPVPA NPGNGMTWQL QDNVSDSFNY
    60 70 80 90 100
    TSSEGNRPTA FTSKWKPSYI NGWTGPGSTI FNAPQAWTNG SQLAIQAQPA
    110 120 130 140 150
    GNGKSYNGII TSKNKIQYPV YMEIKAKIMD QVLANAFWTL TDDETQEIDI
    160 170 180 190 200
    MEGYGSDRGG TWFAQRMHLS HHTFIRNPFT DYQPMGDATW YYNGGTPWRS
    210 220 230 240 250
    AYHRYGCYWK DPFTLEYYID GVKVRTVTRA EIDPNNHLGG TGLNQATNII
    260 270 280 290 300
    IDCENQTDWR PAATQEELAD DSKNIFWVDW IRVYKPVAVS GGGNNGNDGA
    310 320 330 340 350
    TEFQYDLGTD TSAVWPGYTR VSNTTRAGNF GWANTNDIGS RDRGASNGRN
    360 370 380 390 400
    NINRDINFSS QTRFFTQDLS NGTYNVLITF GDTYARKNMN VAAEGQNKLT
    410 420 430 440 450
    NINTNAGQYV SRSFDVNVND GKLDLRFSVG NGGDVWSITR IWIRKVTSNS
    460 470 480 490 500
    ANLLAAKGLT LEDPVETTEF LYPNPAKTDD FVTVPNSEIG SSIIIYNSAG
    510 520 530
    QVVKKVSVVS ENQKISLEGF AKGMYFINLN GQSTKLIVQ
    Length:539
    Mass (Da):60,020
    Last modified:October 19, 2011 - v1
    Checksum:i8D60A87DBF009A44
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti84P → A in AAF21820 (PubMed:15456406).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF098954 Genomic DNA. Translation: AAF21820.1.
    FP476056 Genomic DNA. Translation: CAZ98338.1.

    Genome annotation databases

    EnsemblBacteriaiCAZ98338; CAZ98338; ZOBELLIA_4203.
    KEGGizga:ZOBELLIA_4203.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF098954 Genomic DNA. Translation: AAF21820.1.
    FP476056 Genomic DNA. Translation: CAZ98338.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O4YX-ray1.48A20-295[»]
    1URXX-ray1.70A20-290[»]
    SMRiG0L322.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAZ98338; CAZ98338; ZOBELLIA_4203.
    KEGGizga:ZOBELLIA_4203.

    Phylogenomic databases

    KOiK01219.

    Enzyme and pathway databases

    BRENDAi3.2.1.81. 7557.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR008979. Galactose-bd-like.
    IPR000757. GH16.
    IPR026444. Secre_tail.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 1 hit.
    TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.
    PROSITEiPS51762. GH16_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAGAA_ZOBGA
    AccessioniPrimary (citable) accession number: G0L322
    Secondary accession number(s): Q9RGX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: October 19, 2011
    Last modified: November 2, 2016
    This is version 32 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, Direct protein sequencing, 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.