Alginate lyase - Sphingomonas sp.

Preferred order of sections

Names and origin

Protein names

Submitted name:
Alginate lyase EMBL BAB03312.1

Gene names

Name:

aly EMBL BAB03312.1

Organism

Sphingomonas sp. EMBL BAB03312.1

Taxonomic identifier

28214 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Sphingomonas

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Lyase EMBL BAB03312.1
Technical term	3D-structure PDB 4F10 PDB 4F13 PDB 1QAZ PDB 1HV6 PDB 4E1Y
Gene Ontology (GO)
Biological_process	alginic acid catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular_function	poly(beta-D-mannuronate) lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Active site

294

1

Proton donor/acceptor PDB 1QAZ

Site

239

1

Transition state stabilizer PDB 1QAZ

Site

287

1

Important for catalytic activity PDB 1QAZ

Sequences

Sequence

Length

Mass (Da)

Tools

Q9KWU1 [UniParc].

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

FASTA

641

71,003

        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, 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.
[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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HV6	X-ray	2.00	A	54-402	[»]
1QAZ	X-ray	1.78	A	54-402	[»]
4E1Y	X-ray	2.10	A/B	54-404	[»]
4F10	X-ray	2.20	A/B	54-404	[»]
4F13	X-ray	2.21	A/B	54-404	[»]

ProteinModelPortal

Q9KWU1.

SMR

Q9KWU1. Positions 53-402, 415-641.

ModBase

Search...

Protein family/group databases

CAZy

PL5. Polysaccharide Lyase Family 5.
PL7. Polysaccharide Lyase Family 7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.50.10.110. 1 hit.
2.60.120.200. 1 hit.

InterPro

IPR014895. Alginate_lyase_2.
IPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]

Pfam

PF05426. Alginate_lyase. 1 hit.
PF08787. Alginate_lyase2. 1 hit.
[Graphical view]

SUPFAM

SSF48230. Chondroitin_lyas. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9KWU1.

Entry information

Entry name

Q9KWU1_SPHSX

Accession

Primary (citable) accession number: Q9KWU1

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2000
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)