Chondroitin ABC endolyase 1 precursor

Names and origin

Protein names	Recommended name: Chondroitin ABC endolyase 1 EC=4.2.2.20 Alternative name(s): Chondroitin ABC lyase I Chondroitinase ABC Chondroitin sulfate endolyase Chondroitin ABC eliminase
Organism	Proteus vulgaris
Taxonomic identifier	585 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

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Protein attributes

Sequence length	1021 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Endolytic cleavage of (1->4)-beta-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra- and disaccharides.
Cofactor	Binds 1 sodium or calcium ion per subunit.
Subunit structure	Monomer.
Sequence similarities	Belongs to the polysaccharide lyase 8 family.
Sequence caution	The sequence described in Ref.1 differs from that shown. Reason: Frameshift at positions 494 and 530.

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Ontologies

Keywords
Domain	Signal
Ligand	Calcium Metal-binding Sodium
Molecular function	Lyase
Technical term	3D-structure
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	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate binding Inferred from electronic annotation. Source: InterPro chondroitin-sulfate-ABC endolyase activity Inferred from electronic annotation. Source: EC sodium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Chain

25 – 1021

997

Chondroitin ABC endolyase 1

PRO_0000024929

Sites

Active site

501

1

Probable

Active site

508

1

Probable

Active site

560

1

Probable

Metal binding

43

1

Sodium or calcium; via carbonyl oxygen

Metal binding

70

1

Sodium or calcium; via carbonyl oxygen

Metal binding

73

1

Sodium or calcium; via carbonyl oxygen

Metal binding

211

1

Sodium or calcium

Experimental info

Sequence conflict

125

1

L → P Ref.1

Sequence conflict

317

1

Y → T Ref.1

Sequence conflict

321

1

N → D Ref.1

Sequence conflict

369

1

M → V Ref.1

Sequence conflict

410

1

E → Q Ref.1

Sequence conflict

670

1

A → G Ref.1

Sequence conflict

865 – 866

2

ST → RY Ref.1

Secondary structure

1

.

1021

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P59807-1 [UniParc].

Last modified August 15, 2003. Version 1.
Checksum: A11334EE0A67213A
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FASTA

1,021

115,092

        10         20         30         40         50         60 
MPIFRFTALA MTLGLLSAPY NAMAATSNPA FDPKNLMQSE IYHFAQNNPL ADFSSDKNSI 

        70         80         90        100        110        120 
LTLSDKRSIM GNQSLLWKWK GGSSFTLHKK LIVPTDKEAS KAWGRSSTPV FSFWLYNEKP 

       130        140        150        160        170        180 
IDGYLTIDFG EKLISTSEAQ AGFKVKLDFT GWRAVGVSLN NDLENREMTL NATNTSSDGT 

       190        200        210        220        230        240 
QDSIGRSLGA KVDSIRFKAP SNVSQGEIYI DRIMFSVDDA RYQWSDYQVK TRLSEPEIQF 

       250        260        270        280        290        300 
HNVKPQLPVT PENLAAIDLI RQRLINEFVG GEKETNLALE ENISKLKSDF DALNIHTLAN 

       310        320        330        340        350        360 
GGTQGRHLIT DKQIIIYQPE NLNSQDKQLF DNYVILGNYT TLMFNISRAY VLEKDPTQKA 

       370        380        390        400        410        420 
QLKQMYLLMT KHLLDQGFVK GSALVTTHHW GYSSRWWYIS TLLMSDALKE ANLQTQVYDS 

       430        440        450        460        470        480 
LLWYSREFKS SFDMKVSADS SDLDYFNTLS RQHLALLLLE PDDQKRINLV NTFSHYITGA 

       490        500        510        520        530        540 
LTQVPPGGKD GLRPDGTAWR HEGNYPGYSF PAFKNASQLI YLLRDTPFSV GESGWNNLKK 

       550        560        570        580        590        600 
AMVSAWIYSN PEVGLPLAGR HPFNSPSLKS VAQGYYWLAM SAKSSPDKTL ASIYLAISDK 

       610        620        630        640        650        660 
TQNESTAIFG ETITPASLPQ GFYAFNGGAF GIHRWQDKMV TLKAYNTNVW SSEIYNKDNR 

       670        680        690        700        710        720 
YGRYQSHGVA QIVSNGSQLS QGYQQEGWDW NRMEGATTIH LPLKDLDSPK PHTLMQRGER 

       730        740        750        760        770        780 
GFSGTSSLEG QYGMMAFNLI YPANLERFDP NFTAKKSVLA ADNHLIFIGS NINSSDKNKN 

       790        800        810        820        830        840 
VETTLFQHAI TPTLNTLWIN GQKIENMPYQ TTLQQGDWLI DSNGNGYLIT QAEKVNVSRQ 

       850        860        870        880        890        900 
HQVSAENKNR QPTEGNFSSA WIDHSTRPKD ASYEYMVFLD ATPEKMGEMA QKFRENNGLY 

       910        920        930        940        950        960 
QVLRKDKDVH IILDKLSNVT GYAFYQPASI EDKWIKKVNK PAIVMTHRQK DTLIVSAVTP 

       970        980        990       1000       1010       1020 
DLNMTRQKAA TPVTINVTIN GKWQSADKNS EVKYQVSGDN TELTFTSYFG IPQEIKLSPL 


P

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References

[1]	"Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase." Sato N., Shimada M., Nakajima H., Oda H., Kimura S. Appl. Microbiol. Biotechnol. 41:39-46(1994) [PubMed: 7512814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6896 / IFO 3988 / NCIMB 8065 / NCTC 4636.
[2]	"Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides." Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K., Suzuki S. J. Biol. Chem. 272:9123-9130(1997) [PubMed: 9083041] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 6896 / IFO 3988 / NCIMB 8065 / NCTC 4636.
[3]	"Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution." Huang W., Lunin V.V., Li Y., Suzuki S., Sugiura N., Miyazono H., Cygler M. J. Mol. Biol. 328:623-634(2003) [PubMed: 12706721] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION. Strain: ATCC 6896 / IFO 3988 / NCIMB 8065 / NCTC 4636.

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Cross-references

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HN0	X-ray	1.90	A	1-1021	[»]

ModBase

Search...

Protein family/group databases

CAZy

PL8. Polysaccharide Lyase Family 8.

Enzyme and pathway databases

BRENDA

4.2.2.20. 641.

Family and domain databases

InterPro

IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central.
IPR012329. Lyase_8_N.
IPR015177. Lyase_catalyt.
IPR015176. Lyase_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.
G3DSA:2.60.120.410. Lyase_N. 1 hit.

Pfam

PF02278. Lyase_8. 1 hit.
PF09093. Lyase_catalyt. 1 hit.
PF09092. Lyase_N. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

CABC_PROVU

Accession

Primary (citable) accession number: P59807

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	August 15, 2003
Last modified:	April 14, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families