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Q9F5I8 (CGIA_ALTFO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 5, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iota-carrageenase
EC=3.2.1.157
Gene names
Name:cgiA
OrganismAlteromonas fortis (Alteromonas sp. (strain ATCC 43554))
Taxonomic identifier116059 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta galactans from red algal cell walls, with an inversion of anomeric configuration. Also active against hybrid iota-/nu-carrageenan, not active against kappa- or lambda-carrageenans. Ref.1 Ref.2 UniProtKB Q9F284

Catalytic activity

Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans. Ref.1

Subcellular location

Secreted › extracellular space By similarity UniProtKB Q9F284.

Sequence similarities

Belongs to the glycosyl hydrolase 82 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioniota-carrageenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 491468Iota-carrageenase
PRO_5000065977

Amino acid modifications

Disulfide bond269 ↔ 298 Ref.3 Ref.4
Disulfide bond336 ↔ 360 Ref.3 Ref.4
Disulfide bond408 ↔ 476 Ref.3 Ref.4
Disulfide bond412 ↔ 484 Ref.3 Ref.4

Secondary structure

1 ..................................................................... 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9F5I8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D5912275F06992CF

FASTA49154,795
        10         20         30         40         50         60 
MRLYFRKLWL TNLFLGGALA SSAAIGAVSP KTYKDADFYV APTQQDVNYD LVDDFGANGN 

        70         80         90        100        110        120 
DTSDDSNALQ RAINAISRKP NGGTLLIPNG TYHFLGIQMK SNVHIRVESD VIIKPTWNGD 

       130        140        150        160        170        180 
GKNHRLFEVG VNNIVRNFSF QGLGNGFLVD FKDSRDKNLA VFKLGDVRNY KISNFTIDDN 

       190        200        210        220        230        240 
KTIFASILVD VTERNGRLHW SRNGIIERIK QNNALFGYGL IQTYGADNIL FRNLHSEGGI 

       250        260        270        280        290        300 
ALRMETDNLL MKNYKQGGIR NIFADNIRCS KGLAAVMFGP HFMKNGDVQV TNVSSVSCGS 

       310        320        330        340        350        360 
AVRSDSGFVE LFSPTDEVHT RQSWKQAVES KLGRGCAQTP YARGNGGTRW AARVTQKDAC 

       370        380        390        400        410        420 
LDKAKLEYGI EPGSFGTVKV FDVTARFGYN ADLKQDQLDY FSTSNPMCKR VCLPTKEQWS 

       430        440        450        460        470        480 
KQGQIYIGPS LAAVIDTTPE TSKYDYDVKT FNVKRINFPV NSHKTIDTNT ESSRVCNYYG 

       490 
MSECSSSRWE R

« Hide

References

[1]"iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases."
Barbeyron T., Michel G., Potin P., Henrissat B., Kloareg B.
J. Biol. Chem. 275:35499-35505(2000) [PubMed: 10934194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
[2]"Enzymatic degradation of hybrid iota-/nu-carrageenan by Alteromonas fortis iota-carrageenase."
Jouanneau D., Boulenguer P., Mazoyer J., Helbert W.
Carbohydr. Res. 345:934-940(2010) [PubMed: 20227066] [Abstract]
Cited for: FUNCTION.
[3]"The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide."
Michel G., Chantalat L., Fanchon E., Henrissat B., Kloareg B., Dideberg O.
J. Biol. Chem. 276:40202-40209(2001) [PubMed: 11493601] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 28-491, DISULFIDE BONDS.
[4]"The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae."
Michel G., Helbert W., Kahn R., Dideberg O., Kloareg B.
J. Mol. Biol. 334:421-433(2003) [PubMed: 14623184] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-491 IN COMPLEX WITH SUBSTRATE, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ272076 Genomic DNA. Translation: CAC07801.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H80X-ray1.60A/B28-491[»]
1KTWX-ray2.00A/B28-491[»]
3LMWX-ray2.60A/B27-491[»]
ProteinModelPortalQ9F5I8.
SMRQ9F5I8. Positions 28-491.
ModBaseSearch...

Protein family/group databases

CAZyGH82. Glycoside Hydrolase Family 82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCGIA_ALTFO
AccessionPrimary (citable) accession number: Q9F5I8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 1, 2001
Last modified: April 5, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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