Reviewed, UniProtKB/Swiss-Prot Q8L0V4 (CHS_ECOLX)

Names and origin

Protein names

Recommended name:
    Chondroitin synthase
      Short name=CS
Alternative name(s):
    Chondroitin polymerase
Including the following 2 domains:
    1- Recommended name:
            Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase
              EC=2.4.1.175
        Alternative name(s):
            UDP-GalNAc transferase
    2- Recommended name:
            N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase
              EC=2.4.1.226
        Alternative name(s):
            UDP-GlcUA transferase

Gene names

Name:

kfoC

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	686 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the polymerization of chondroitin, a polysaccharide composed of a repeating disaccharide of N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcUA) units. Each unit has the composition in beta-(1->4)-GlcUA-beta-(1->3)-GalNAc.
Catalytic activity	UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan. UDP-N-acetyl-D-galactosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan = UDP + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan.
Cofactor	Manganese.
Sequence similarities	Belongs to the glycosyltransferase 2 family. CS/HAS subfamily.
Biophysicochemical properties	Kinetic parameters: KM=3.44 µM for UDP-GlcUA KM=31.6 µM for UDP-GalNAc pH dependence: Optimum pH is 7-7.5. Temperature dependence: Optimum temperature is 30 degrees Celsius for highest reaction speed, and 25 degrees Celsius to obtain highest molecular weight of product chondroitin.

Ontologies

Keywords
Domain	Repeat
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Molecular function	N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity Inferred from electronic annotation. Source: EC glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 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

Chain

1 – 686

686

Chondroitin synthase

PRO_0000059257

Regions

Region

143 – 317

175

A1

Region

424 – 596

173

A2

Secondary structure

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686

Helix Strand Turn

Details...

Helix

65 – 73

9

Helix

81 – 94

14

Turn

130 – 132

3

Beta strand

153 – 160

8

Helix

162 – 173

12

Beta strand

182 – 187

6

Helix

194 – 199

6

Turn

200 – 204

5

Beta strand

207 – 212

6

Helix

219 – 224

6

Beta strand

232 – 237

6

Beta strand

242 – 244

3

Helix

248 – 258

11

Beta strand

262 – 265

4

Beta strand

267 – 271

5

Helix

278 – 283

6

Helix

287 – 289

3

Helix

313 – 319

7

Turn

320 – 325

6

Helix

329 – 332

4

Beta strand

338 – 341

4

Helix

343 – 347

5

Turn

362 – 364

3

Helix

368 – 371

4

Beta strand

375 – 380

6

Beta strand

382 – 387

6

Turn

408 – 412

5

Turn

414 – 417

4

Turn

423 – 425

3

Beta strand

433 – 442

10

Turn

444 – 446

3

Helix

447 – 455

9

Beta strand

456 – 458

3

Beta strand

461 – 468

8

Helix

475 – 483

9

Beta strand

489 – 493

5

Helix

502 – 509

8

Helix

528 – 538

11

Beta strand

543 – 552

10

Beta strand

558 – 560

3

Helix

570 – 573

4

Beta strand

583 – 586

4

Helix

587 – 590

4

Helix

604 – 612

9

Beta strand

618 – 629

12

Helix

640 – 654

15

Beta strand

662 – 668

7

Beta strand

677 – 681

5

Sequences

	Sequence		Length	Mass (Da)
	Q8L0V4-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 6FB941623D9EC9D4	FASTA	686	79,257
	10 20 30 40 50 60 MSILNQAINL YKNKNYRQAL SLFEKVAEIY DVSWVEANIK LCQTALNLSE EVDKLNRKAV 70 80 90 100 110 120 IDIDAATKIM CSNAKAISLN EVEKNEIISK YREITAKKSE RAELKEVEPI PLDWPSDLTL 130 140 150 160 170 180 PPLPESTNDY VWAGKRKELD DYPRKQLIID GLSIVIPTYN RAKILAITLA CLCNQKTIYD 190 200 210 220 230 240 YEVIVADDGS KENIEEIVRE FESLLNIKYV RQKDYGYQLC AVRNLGLRAA KYNYVAILDC 250 260 270 280 290 300 DMAPNPLWVQ SYMELLAVDD NVALIGPRKY IDTSKHTYLD FLSQKSLINE IPEIITNNQV 310 320 330 340 350 360 AGKVEQNKSV DWRIEHFKNT DNLRLCNTPF RFFSGGNVAF AKKWLFRAGW FDEEFTHWGG 370 380 390 400 410 420 EDNEFGYRLY REGCYFRSVE GAMAYHQEPP GKENETDRAA GKNITVQLLQ QKVPYFYRKK 430 440 450 460 470 480 EKIESATLKR VPLVSIYIPA YNCSKYIVRC VESALNQTIT DLEVCICDDG STDDTLRILQ 490 500 510 520 530 540 EHYANHPRVR FISQKNKGIG SASNTAVRLC RGFYIGQLDS DDFLEPDAVE LCLDEFRKDL 550 560 570 580 590 600 SLACVYTTNR NIDREGNLIS NGYNWPIYSR EKLTSAMICH HFRMFTARAW NLTEGFNESI 610 620 630 640 650 660 SNAVDYDMYL KLSEVGPFKH INKICYNRVL HGENTSIKKL DIQKENHFKV VNESLSRLGI 670 680 KKYKYSPLTN LNECRKYTWE KIENDL

References

[1]

"Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4." Ninomiya T., Sugiura N., Tawada A., Sugimoto K., Watanabe H., Kimata K. J. Biol. Chem. 277:21567-21575(2002) [PubMed: 11943778] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: O5:K4(L):H4 / ATCC 23502.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB079602 Genomic DNA. Translation: BAC00523.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z86	X-ray	2.40	A/B/C/D	58-682	[»]
2Z87	X-ray	3.00	A/B	59-682	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT2. Glycosyltransferase Family 2.

Enzyme and pathway databases

BRENDA

2.4.1.175. 246.
2.4.1.226. 246.

Family and domain databases

InterPro

IPR001173. Glyco_trans_2.
[Graphical view]

Pfam

PF00535. Glycos_transf_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHS_ECOLX

Accession

Primary (citable) accession number: Q8L0V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2002
Last modified:	September 1, 2009
This is version 24 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)