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Q9KWU1 (Q9KWU1_SPHSX) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 56. Feed History...

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

Names and origin

Protein names
Gene names
Name:aly EMBL BAB03312.1
OrganismSphingomonas sp. EMBL BAB03312.1
Taxonomic identifier28214 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Molecular functionLyase EMBL BAB03312.1
   Technical term3D-structure PDB 4F10 PDB 4F13 PDB 1QAZ PDB 1HV6 PDB 4E1Y
Gene Ontology (GO)
   Biological_processalginic acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionpoly(beta-D-mannuronate) lyase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region233 – 2353Sulfate 2 binding PDB 1QAZ PDB 1HV6

Sites

Active site2941Proton donor/acceptor PDB 1QAZ
Binding site1141Sulfate 1 PDB 1QAZ
Site2391Transition state stabilizer PDB 1QAZ
Site2871Important for catalytic activity PDB 1QAZ

Sequences

Sequence LengthMass (Da)Tools
Q9KWU1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6C3C655070B7AD01

FASTA64171,003
        10         20         30         40         50         60 
MPLACLATTR VGAAREKSGD SSMFDIPFPG HGRRLAVAAL AFAGCAFAGS LQAHPFDQAV 

        70         80         90        100        110        120 
VKDPTASYVD VKARRTFLQS GQLDDRLKAA LPKEYDCTTE ATPNPQQGEM VIPRRYLSGN 

       130        140        150        160        170        180 
HGPVNPDYEP VVTLYRDFEK ISATLGNLYV ATGKPVYATC LLNMLDKWAK ADALLNYDPK 

       190        200        210        220        230        240 
SQSWYQVEWS AATAAFALST MMAEPNVDTA QRERVVKWLN RVARHQTSFP GGDTSCCNNH 

       250        260        270        280        290        300 
SYWRGQEATI IGVISKDDEL FRWGLGRYVQ AMGLINEDGS FVHEMTRHEQ SLHYQNYAML 

       310        320        330        340        350        360 
PLTMIAETAS RQGIDLYAYK ENGRDIHSAR KFVFAAVKNP DLIKKYASEP QDTRAFKPGR 

       370        380        390        400        410        420 
GDLNWIEYQR ARFGFADELG FMTVPIFDPR TGGSGTLLAY KPQGAAAQAP VSAPAAAHSS 

       430        440        450        460        470        480 
IDLSKWKLQI PVDPIDVATR DLLKGYQDKY FYVDKDGSLA FWCPASGFKT TANTKYPRSE 

       490        500        510        520        530        540 
LREMLDPDNH AVNWGWQGTH EMNLRGAVMH VSPSGKTIVM QIHAVMPDGS NAPPLVKGQF 

       550        560        570        580        590        600 
YKNTLDFLVK NSAAGGKDTH YVFEGIELGK PYDAQIKVVD GVLSMTVNGQ TKTVDFVAKD 

       610        620        630        640 
AGWKDLKFYF KAGNYLQDRQ ADGSDTSALV KLYKLDVKHS S 

« Hide

References

[1]"Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 A resolution."
Yoon H.J., Mikami B., Hashimoto W., Murata K.
J. Mol. Biol. 290:505-514(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 54-402 IN COMPLEX WITH SULFATE, ACTIVE SITE.
[2]"A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules."
Momma K., Okamoto M., Mishima Y., Mori S., Hashimoto W., Murata K.
J. Bacteriol. 182:3998-4004(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A1 EMBL BAB03312.1.
[3]"Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution."
Yoon H.J., Hashimoto W., Miyake O., Murata K., Mikami B.
J. Mol. Biol. 307:9-16(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 54-402 IN COMPLEX WITH SULFATE.
[4]"Induced-fit motion of a lid loop involved in catalysis in alginate lyase A1-III."
Mikami B., Ban M., Suzuki S., Yoon H.J., Miyake O., Yamasaki M., Ogura K., Maruyama Y., Hashimoto W., Murata K.
Acta Crystallogr. D 68:1207-1216(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 54-404.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011415 Genomic DNA. Translation: BAB03312.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HV6X-ray2.00A54-402[»]
1QAZX-ray1.78A54-402[»]
4E1YX-ray2.10A/B54-404[»]
4F10X-ray2.20A/B54-404[»]
4F13X-ray2.21A/B54-404[»]
ProteinModelPortalQ9KWU1.
SMRQ9KWU1. Positions 53-402, 415-641.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyPL5. Polysaccharide Lyase Family 5.
PL7. Polysaccharide Lyase Family 7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.110. 1 hit.
2.60.120.200. 1 hit.
InterProIPR014895. Alginate_lyase_2.
IPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PfamPF05426. Alginate_lyase. 1 hit.
PF08787. Alginate_lyase2. 1 hit.
[Graphical view]
SUPFAMSSF48230. SSF48230. 1 hit.
SSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9KWU1.

Entry information

Entry nameQ9KWU1_SPHSX
AccessionPrimary (citable) accession number: Q9KWU1
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)