Xanthan lyase - Bacillus sp. (strain GL1)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Xanthan lyase EMBL BAB21059.1

Gene names

Name:

xly EMBL BAB21059.1

Organism

Bacillus sp. (strain GL1) EMBL BAB21059.1

Taxonomic identifier

84635 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	930 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1J0N PDB 1J0M PDB 1X1J Metal-binding PDB 1J0N PDB 1J0M PDB 1X1J
Molecular function	Lyase EMBL BAB21059.1
Technical term	3D-structure PDB 2E22 PDB 1J0N PDB 1J0M PDB 1X1J PDB 2E24 PDB 1X1I PDB 1X1H
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro carbon-oxygen lyase activity, acting on polysaccharides Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

515

1

Calcium PDB 1J0N PDB 1J0M PDB 1X1J

Metal binding

516

1

Calcium PDB 1J0N PDB 1J0M PDB 1X1J

Metal binding

517

1

Calcium PDB 1J0N PDB 1J0M PDB 1X1J

Metal binding

676

1

Calcium PDB 1J0N PDB 1J0M PDB 1X1J

Binding site

148

1

Mannose PDB 2E22

Binding site

255

1

Mannose PDB 2E22

Binding site

309

1

Mannose PDB 2E22

Binding site

313

1

Mannose PDB 2E22

Sequences

Sequence

Length

Mass (Da)

Tools

Q9AQS0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5E8B69D3E94019C4
Show »

FASTA

930

99,313

        10         20         30         40         50         60 
MLSGILIAAL LMTLWGGWQP DIAHASDEFD ALRIKWATLL TGGPALDPAD SDIAARTDKL 

        70         80         90        100        110        120 
AQDANDYWED MDLSSSRTYI WYALRGNGTS DNVNAVYERL RTMALAATTV GSSLYGNADL 

       130        140        150        160        170        180 
KEDILDALDW LYVNSYNSTR SRSAYNWWHW QLGIPMSLND IAVLLYDDIS AARMATYMDT 

       190        200        210        220        230        240 
IDYFTPSIGL TGANRAWQAI VVGVRAVIVK DAVKLAAARN GLSGTGIFPY ATGGDGFYAD 

       250        260        270        280        290        300 
GSFVQHTTFA YTGGYGSSVL ETTANLMYLL SGSTWSVSDP NQSNVWQWIY EAYRPLLYKG 

       310        320        330        340        350        360 
AMMDMVRGRE ISRSYAQDHA VGHGIVASIV RLAQFAPAPH AAAFKQIAKR VIQEDTFSSF 

       370        380        390        400        410        420 
YGDVSTDTIR LAKAIVDDPS IAPAAAPNLY KQYAAMDRAV LQRPGFALGL ALYSTRISSY 

       430        440        450        460        470        480 
ESINSENGRG WYTGAGATYL YNQDLAQYSE DYWPTVDAYR IPGTTVASGT PIASGTGTSS 

       490        500        510        520        530        540 
WTGGVSLAGQ YGASGMDLSY GAYNLSARKS WFMFDDEIVA LGSGISSTAG IPIETVVDNR 

       550        560        570        580        590        600 
KLNGAGDNAW TANGAALSTG LGVAQTLTGV NWVHLAGNTA DGSDIGYYFP GGATLQTKRE 

       610        620        630        640        650        660 
ARTGTWKQIN NRPATPSTAV TRNYETMWID HGTNPSGASY GYVLLPNKTS AQVGAYAADP 

       670        680        690        700        710        720 
AIEIVVNTSG VQSVKEKTLG LVGANFWTDT TQTADLITSN KKASVMTREI ADERLEASVS 

       730        740        750        760        770        780 
DPTQANNGTI AIELARSAEG YSADPGITVT QLAPTIKFTV NVNGAKGKSF HASFQLGEDT 

       790        800        810        820        830        840 
SGPVDPGEPE LPSVIVDNAD SAGVTRTGTW KTASTQTDRY GANYLHDDNA GKGTKSVTFT 

       850        860        870        880        890        900 
PNLPIAGSYE VYLMWPAHFN REDAVQVDVG HASGTTRTAV DQRSGGGVWH SIGTYEFLAG 

       910        920        930 
SGGSVTIRND ALGSPDGYVV ADAVKFVAVG

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References

[1]	"Polysaccharide lyase: molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1." Hashimoto W., Miki H., Tsuchiya N., Nankai H., Murata K. Appl. Environ. Microbiol. 67:713-720(2001) [PubMed: 11157235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: GL1 EMBL BAB21059.1.
[2]	"Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan." Hashimoto W., Nankai H., Mikami B., Murata K. J. Biol. Chem. 278:7663-7673(2003) [PubMed: 12475987] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-777 IN COMPLEX WITH CALCIUM.
[3]	"A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan." Maruyama Y., Mikami B., Hashimoto W., Murata K. Biochemistry 46:781-791(2007) [PubMed: 17223699] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-777 IN COMPLEX WITH MANNOSE.
[4]	"Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism." Maruyama Y., Hashimoto W., Mikami B., Murata K. J. Mol. Biol. 350:974-986(2005) [PubMed: 15979090] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 26-777 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB037178 Genomic DNA. Translation: BAB21059.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J0M	X-ray	2.30	A	26-777	[»]
1J0N	X-ray	2.40	A	26-777	[»]
1X1H	X-ray	2.30	A	26-777	[»]
1X1I	X-ray	1.80	A	26-777	[»]
1X1J	X-ray	2.10	A	26-777	[»]
2E22	X-ray	2.40	A	26-777	[»]
2E24	X-ray	2.15	A	26-777	[»]

ProteinModelPortal

Q9AQS0.

SMR

Q9AQS0. Positions 26-777.

ModBase

Search...

Protein family/group databases

CAZy

PL8. Polysaccharide Lyase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008929. Chondroitin_lyas.
IPR011013. Glyco_hydro-type_carb-bd.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view]

Gene3D

G3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
G3DSA:2.60.220.10. Lyase_8_C. 1 hit.
G3DSA:1.50.10.100. Lyase_8_N. 1 hit.

Pfam

PF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]

SUPFAM

SSF48230. Chondroitin_lyas. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
SSF49863. Lyase_like_C. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q9AQS0_BACGL

Accession

Primary (citable) accession number: Q9AQS0

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	July 27, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)