Reviewed, UniProtKB/Swiss-Prot Q59288 (CSLA_PEDHD)

Names and origin

Protein names

Recommended name:
    Chondroitinase-AC
    EC=4.2.2.5
Alternative name(s):
    Chondroitin-AC lyase
    Chondroitin sulfate AC lyase
    Chondroitin-AC eliminase

Gene names

Name:	cslA
Synonyms:	chnAC
Ordered Locus Names:	Phep_0786

Organism

Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) [Complete proteome] [HAMAP]

Taxonomic identifier

485917 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Monomer.
Sequence similarities	Belongs to the polysaccharide lyase 8 family.

Ontologies

Keywords
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome
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 AC lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 700

678

Chondroitinase-AC

PRO_0000024927

Sites

Active site

225

1

Active site

234

1

Active site

288

1

Metal binding

405

1

Calcium

Metal binding

407

1

Calcium

Metal binding

416

1

Calcium

Metal binding

417

1

Calcium; via carbonyl oxygen

Amino acid modifications

Glycosylation

328

1

O-linked (Man...)

Glycosylation

455

1

O-linked (Man...)

Secondary structure

1

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700

Helix Strand Turn

Details...

Helix

27 – 39

13

Helix

46 – 56

11

Beta strand

73 – 75

3

Helix

79 – 93

15

Turn

98 – 101

4

Helix

103 – 119

17

Helix

126 – 130

5

Helix

132 – 143

12

Helix

144 – 146

3

Beta strand

147 – 149

3

Helix

153 – 161

9

Helix

168 – 170

3

Helix

173 – 189

17

Helix

193 – 204

12

Beta strand

207 – 217

11

Beta strand

225 – 227

3

Turn

231 – 233

3

Helix

234 – 249

16

Helix

258 – 270

13

Helix

273 – 275

3

Helix

283 – 285

3

Helix

287 – 291

5

Turn

293 – 296

4

Helix

299 – 301

3

Helix

302 – 311

10

Helix

313 – 315

3

Helix

316 – 326

11

Turn

332 – 335

4

Beta strand

339 – 343

5

Turn

344 – 347

4

Beta strand

348 – 353

6

Beta strand

356 – 361

6

Turn

381 – 384

4

Beta strand

385 – 394

10

Helix

395 – 397

3

Helix

401 – 403

3

Beta strand

413 – 415

3

Beta strand

425 – 427

3

Beta strand

436 – 440

5

Beta strand

445 – 453

9

Beta strand

456 – 464

9

Beta strand

469 – 478

10

Beta strand

480 – 492

13

Beta strand

497 – 499

3

Beta strand

502 – 504

3

Beta strand

509 – 514

6

Beta strand

519 – 522

4

Beta strand

525 – 528

4

Beta strand

533 – 538

6

Beta strand

541 – 546

6

Turn

547 – 549

3

Beta strand

557 – 572

16

Beta strand

574 – 584

11

Helix

590 – 593

4

Helix

596 – 598

3

Beta strand

601 – 614

14

Turn

615 – 618

4

Beta strand

619 – 632

14

Beta strand

635 – 641

7

Beta strand

643 – 648

6

Beta strand

655 – 659

5

Beta strand

666 – 674

9

Turn

675 – 677

3

Beta strand

680 – 686

7

Helix

690 – 692

3

Sequences

	Sequence		Length	Mass (Da)
	Q59288-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C36B608FCAFFC656	FASTA	700	79,694
	10 20 30 40 50 60 MKKLFVTCIV FFSILSPALL IAQQTGTAEL IMKRVMLDLK KPLRNMDKVA EKNLNTLQPD 70 80 90 100 110 120 GSWKDVPYKD DAMTNWLPNN HLLQLETIIQ AYIEKDSHYY GDDKVFDQIS KAFKYWYDSD 130 140 150 160 170 180 PKSRNWWHNE IATPQALGEM LILMRYGKKP LDEALVHKLT ERMKRGEPEK KTGANKTDIA 190 200 210 220 230 240 LHYFYRALLT SDEALLSFAV KELFYPVQFV HYEEGLQYDY SYLQHGPQLQ ISSYGAVFIT 250 260 270 280 290 300 GVLKLANYVR DTPYALSTEK LAIFSKYYRD SYLKAIRGSY MDFNVEGRGV SRPDILNKKA 310 320 330 340 350 360 EKKRLLVAKM IDLKHTEEWA DAIARTDSTV AAGYKIEPYH HQFWNGDYVQ HLRPAYSFNV 370 380 390 400 410 420 RMVSKRTRRS ESGNKENLLG RYLSDGATNI QLRGPEYYNI MPVWEWDKIP GITSRDYLTD 430 440 450 460 470 480 RPLTKLWGEQ GSNDFAGGVS DGVYGASAYA LDYDSLQAKK AWFFFDKEIV CLGAGINSNA 490 500 510 520 530 540 PENITTTLNQ SWLNGPVIST AGKTGRGKIT TFKAQGQFWL LHDAIGYYFP EGANLSLSTQ 550 560 570 580 590 600 SQKGNWFHIN NSHSKDEVSG DVFKLWINHG ARPENAQYAY IVLPGINKPE EIKKYNGTAP 610 620 630 640 650 660 KVLANTNQLQ AVYHQQLDMV QAIFYTAGKL SVAGIEIETD KPCAVLIKHI NGKQVIWAAD 670 680 690 700 PLQKEKTAVL SIRDLKTGKT NRVKIDFPQQ EFAGATVELK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum." Tkalec A.L., Fink D., Blain F., Zhang-Sun G., Laliberte M., Bennett D.C., Gu K., Zimmermann J.J.F., Su H. Appl. Environ. Microbiol. 66:29-35(2000) [PubMed: 10618199] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Pedobacter heparinus type strain (HIM 762-3T)." Han C., Spring S., Lapidus A., Glavina del Rio T., Tice H., Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A. , Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goeker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.-P., Detter J.C. Stand. Genomic Sci. 1:54-62(2009) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes." Fethiere J., Eggimann B., Cygler M. J. Mol. Biol. 288:635-647(1999) [PubMed: 10329169] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[4]	"Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis." Huang W., Boju L., Tkalec A.L., Su H., Yang H.O., Gunay N.S., Linhardt R.J., Kim Y.S., Matte A., Cygler M. Biochemistry 40:2359-2372(2001) [PubMed: 11327856] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U27583 Genomic DNA. Translation: AAC83383.1.
CP001681 Genomic DNA. Translation: ACU03008.1.

RefSeq

YP_003091070.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CB8	X-ray	1.90	A	23-700	[»]
1HM2	X-ray	2.00	A	1-700	[»]
1HM3	X-ray	2.10	A	1-700	[»]
1HMU	X-ray	2.00	A	1-700	[»]
1HMW	X-ray	2.30	A	1-700	[»]

ModBase

Search...

Protein family/group databases

CAZy

PL8. Polysaccharide Lyase Family 8.

Genome annotation databases

GeneID

8251875.

GenomeReviews

Gene locus Phep_0786 in contig CP001681_GR.

Organism-specific databases

CMR

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]

ProtoNet

Search...

Entry information

Entry name

CSLA_PEDHD

Accession

Primary (citable) accession number: Q59288
Secondary accession number(s): C6Y215

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	December 15, 2009
This is version 54 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)