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Protein

Alginate lyase

Gene

algL

Organism
Azotobacter vinelandii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. Splits ManA-ManA and ManA-GulA bonds, but not GulA-ManA or GulA-GulA bonds. Also cleaves acetylated residues (PubMed:9683471). May serve to degrade mislocalized alginate that is trapped in the periplasmic space (By similarity).UniRule annotation1 Publication

Catalytic activityi

Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.UniRule annotation1 Publication

pH dependencei

Optimum pH is 8.1-8.4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei253 – 2531SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BRENDAi4.2.2.3. 49.

Protein family/group databases

CAZyiPL5. Polysaccharide Lyase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Alginate lyase1 PublicationUniRule annotation (EC:4.2.2.3UniRule annotation1 Publication)
Alternative name(s):
Poly(beta-D-mannuronate) lyaseUniRule annotation
Gene namesi
Name:algL1 PublicationUniRule annotation
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Subcellular locationi

  • Periplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323UniRule annotationAdd
BLAST
Chaini24 – 374351Alginate lyasePRO_0000024916Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi322710.Avin_10900.

Structurei

3D structure databases

ProteinModelPortaliO52195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 632Substrate bindingUniRule annotation
Regioni135 – 1362Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the polysaccharide lyase 5 family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105FN4. Bacteria.
ENOG4111N6J. LUCA.

Family and domain databases

Gene3Di1.50.10.110. 1 hit.
HAMAPiMF_00557. Alginate_lyase.
InterProiIPR022859. Alginate_lyase.
IPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
[Graphical view]
PfamiPF05426. Alginate_lyase. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O52195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKTRLALSC LLGSLLLSGA VHAAEALVPP KGYYAPVDIR KGEAPACPVV
60 70 80 90 100
PEPFTGELVF RSKYEGSDAA RSTLNEEAEK AFRTKTAPIT QIERGVSRMV
110 120 130 140 150
MRYMEKGRAG DLECTLAWLD AWAEDGALLT TEYNHTGKSM RKWALGSLAG
160 170 180 190 200
AYLRLKFSSS QPLAAYPEQA RRIESWFAKV GDQVIKDWSD LPLKRINNHS
210 220 230 240 250
YWAAWAVMAA GVATNRRPLF DWAVEQFHIA AGQVDSNGFL PNELKRRQRA
260 270 280 290 300
LAYHNYSLPP LMMVAAFALA NGVDLRGDND GALGRLAGNV LAGVEKPEPF
310 320 330 340 350
AERAGDEDQD MEDLETDAKF SWLEPYCALY SCSPALRERK AEMGPFKNFR
360 370
LGGDVTRIFD PAEKSPRSTV GKRD
Length:374
Mass (Da):41,404
Last modified:June 1, 1998 - v1
Checksum:i89FAF1CC0CA74961
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027499 Genomic DNA. Translation: AAC04567.1.
AF037600 Genomic DNA. Translation: AAC32313.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027499 Genomic DNA. Translation: AAC04567.1.
AF037600 Genomic DNA. Translation: AAC32313.1.

3D structure databases

ProteinModelPortaliO52195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi322710.Avin_10900.

Protein family/group databases

CAZyiPL5. Polysaccharide Lyase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105FN4. Bacteria.
ENOG4111N6J. LUCA.

Enzyme and pathway databases

BRENDAi4.2.2.3. 49.

Family and domain databases

Gene3Di1.50.10.110. 1 hit.
HAMAPiMF_00557. Alginate_lyase.
InterProiIPR022859. Alginate_lyase.
IPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
[Graphical view]
PfamiPF05426. Alginate_lyase. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Vazquez R.A., Alvarado D.A., Guzman J., Soberon-Chavez G., Espin G.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 9046.
  2. "Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase."
    Ertesvag H., Erlien F., Skjak-Braek G., Rehm B.H., Valla S.
    J. Bacteriol. 180:3779-3784(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: E.

Entry informationi

Entry nameiALGL_AZOVI
AccessioniPrimary (citable) accession number: O52195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 11, 2016
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

Documents

  1. 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.