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Protein

Chondroitin synthase

Gene

kfoC

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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-alpha-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.

Cofactori

Kineticsi

  1. KM=3.44 µM for UDP-GlcUA
  2. KM=31.6 µM for UDP-GalNAc

    pH dependencei

    Optimum pH is 7-7.5.

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius for highest reaction speed, and 25 degrees Celsius to obtain highest molecular weight of product chondroitin.

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.175. 2026.

    Protein family/group databases

    CAZyiGT2. Glycosyltransferase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chondroitin synthase
    Short name:
    CS
    Alternative name(s):
    Chondroitin polymerase
    Including the following 2 domains:
    Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase (EC:2.4.1.175)
    Alternative name(s):
    UDP-GalNAc transferase
    N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC:2.4.1.226)
    Alternative name(s):
    UDP-GlcUA transferase
    Gene namesi
    Name:kfoC
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000592571 – 686Chondroitin synthaseAdd BLAST686

    Proteomic databases

    PRIDEiQ8L0V4.

    Structurei

    Secondary structure

    1686
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi65 – 73Combined sources9
    Beta strandi75 – 77Combined sources3
    Helixi81 – 94Combined sources14
    Helixi130 – 134Combined sources5
    Beta strandi152 – 160Combined sources9
    Helixi162 – 173Combined sources12
    Beta strandi181 – 189Combined sources9
    Helixi194 – 199Combined sources6
    Turni200 – 204Combined sources5
    Beta strandi207 – 212Combined sources6
    Helixi219 – 229Combined sources11
    Beta strandi232 – 238Combined sources7
    Beta strandi242 – 244Combined sources3
    Helixi248 – 258Combined sources11
    Beta strandi262 – 265Combined sources4
    Beta strandi268 – 271Combined sources4
    Helixi273 – 275Combined sources3
    Helixi278 – 283Combined sources6
    Helixi287 – 289Combined sources3
    Beta strandi300 – 302Combined sources3
    Beta strandi303 – 307Combined sources5
    Helixi313 – 319Combined sources7
    Turni320 – 325Combined sources6
    Helixi329 – 332Combined sources4
    Beta strandi337 – 341Combined sources5
    Helixi343 – 348Combined sources6
    Helixi361 – 371Combined sources11
    Beta strandi375 – 378Combined sources4
    Helixi380 – 382Combined sources3
    Beta strandi384 – 387Combined sources4
    Beta strandi391 – 393Combined sources3
    Turni408 – 412Combined sources5
    Turni414 – 417Combined sources4
    Turni423 – 425Combined sources3
    Beta strandi433 – 442Combined sources10
    Turni444 – 446Combined sources3
    Helixi447 – 455Combined sources9
    Beta strandi456 – 458Combined sources3
    Beta strandi461 – 470Combined sources10
    Beta strandi472 – 474Combined sources3
    Helixi475 – 483Combined sources9
    Beta strandi489 – 494Combined sources6
    Helixi499 – 509Combined sources11
    Beta strandi512 – 517Combined sources6
    Helixi528 – 538Combined sources11
    Beta strandi543 – 552Combined sources10
    Beta strandi558 – 561Combined sources4
    Helixi570 – 573Combined sources4
    Beta strandi583 – 586Combined sources4
    Helixi587 – 590Combined sources4
    Turni591 – 594Combined sources4
    Helixi604 – 612Combined sources9
    Turni613 – 615Combined sources3
    Beta strandi618 – 629Combined sources12
    Helixi640 – 654Combined sources15
    Turni655 – 659Combined sources5
    Beta strandi662 – 668Combined sources7
    Beta strandi677 – 681Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Z86X-ray2.40A/B/C/D58-682[»]
    2Z87X-ray3.00A/B59-682[»]
    ProteinModelPortaliQ8L0V4.
    SMRiQ8L0V4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8L0V4.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni143 – 317A1Add BLAST175
    Regioni424 – 596A2Add BLAST173

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    KOiK13500.

    Family and domain databases

    Gene3Di3.90.550.10. 2 hits.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 2 hits.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q8L0V4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSILNQAINL YKNKNYRQAL SLFEKVAEIY DVSWVEANIK LCQTALNLSE
    60 70 80 90 100
    EVDKLNRKAV IDIDAATKIM CSNAKAISLN EVEKNEIISK YREITAKKSE
    110 120 130 140 150
    RAELKEVEPI PLDWPSDLTL PPLPESTNDY VWAGKRKELD DYPRKQLIID
    160 170 180 190 200
    GLSIVIPTYN RAKILAITLA CLCNQKTIYD YEVIVADDGS KENIEEIVRE
    210 220 230 240 250
    FESLLNIKYV RQKDYGYQLC AVRNLGLRAA KYNYVAILDC DMAPNPLWVQ
    260 270 280 290 300
    SYMELLAVDD NVALIGPRKY IDTSKHTYLD FLSQKSLINE IPEIITNNQV
    310 320 330 340 350
    AGKVEQNKSV DWRIEHFKNT DNLRLCNTPF RFFSGGNVAF AKKWLFRAGW
    360 370 380 390 400
    FDEEFTHWGG EDNEFGYRLY REGCYFRSVE GAMAYHQEPP GKENETDRAA
    410 420 430 440 450
    GKNITVQLLQ QKVPYFYRKK EKIESATLKR VPLVSIYIPA YNCSKYIVRC
    460 470 480 490 500
    VESALNQTIT DLEVCICDDG STDDTLRILQ EHYANHPRVR FISQKNKGIG
    510 520 530 540 550
    SASNTAVRLC RGFYIGQLDS DDFLEPDAVE LCLDEFRKDL SLACVYTTNR
    560 570 580 590 600
    NIDREGNLIS NGYNWPIYSR EKLTSAMICH HFRMFTARAW NLTEGFNESI
    610 620 630 640 650
    SNAVDYDMYL KLSEVGPFKH INKICYNRVL HGENTSIKKL DIQKENHFKV
    660 670 680
    VNESLSRLGI KKYKYSPLTN LNECRKYTWE KIENDL
    Length:686
    Mass (Da):79,257
    Last modified:October 1, 2002 - v1
    Checksum:i6FB941623D9EC9D4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB079602 Genomic DNA. Translation: BAC00523.1.
    RefSeqiWP_000025667.1. NZ_LVSL01000002.1.

    Genome annotation databases

    KEGGiag:BAC00523.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB079602 Genomic DNA. Translation: BAC00523.1.
    RefSeqiWP_000025667.1. NZ_LVSL01000002.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Z86X-ray2.40A/B/C/D58-682[»]
    2Z87X-ray3.00A/B59-682[»]
    ProteinModelPortaliQ8L0V4.
    SMRiQ8L0V4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGT2. Glycosyltransferase Family 2.

    Proteomic databases

    PRIDEiQ8L0V4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAC00523.

    Phylogenomic databases

    KOiK13500.

    Enzyme and pathway databases

    BRENDAi2.4.1.175. 2026.

    Miscellaneous databases

    EvolutionaryTraceiQ8L0V4.

    Family and domain databases

    Gene3Di3.90.550.10. 2 hits.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 2 hits.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHS_ECOLX
    AccessioniPrimary (citable) accession number: Q8L0V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: October 1, 2002
    Last modified: November 2, 2016
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.