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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 686686Chondroitin synthasePRO_0000059257Add
    BLAST

    Proteomic databases

    PRIDEiQ8L0V4.

    Structurei

    Secondary structure

    1
    686
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 739Combined sources
    Beta strandi75 – 773Combined sources
    Helixi81 – 9414Combined sources
    Helixi130 – 1345Combined sources
    Beta strandi152 – 1609Combined sources
    Helixi162 – 17312Combined sources
    Beta strandi181 – 1899Combined sources
    Helixi194 – 1996Combined sources
    Turni200 – 2045Combined sources
    Beta strandi207 – 2126Combined sources
    Helixi219 – 22911Combined sources
    Beta strandi232 – 2387Combined sources
    Beta strandi242 – 2443Combined sources
    Helixi248 – 25811Combined sources
    Beta strandi262 – 2654Combined sources
    Beta strandi268 – 2714Combined sources
    Helixi273 – 2753Combined sources
    Helixi278 – 2836Combined sources
    Helixi287 – 2893Combined sources
    Beta strandi300 – 3023Combined sources
    Beta strandi303 – 3075Combined sources
    Helixi313 – 3197Combined sources
    Turni320 – 3256Combined sources
    Helixi329 – 3324Combined sources
    Beta strandi337 – 3415Combined sources
    Helixi343 – 3486Combined sources
    Helixi361 – 37111Combined sources
    Beta strandi375 – 3784Combined sources
    Helixi380 – 3823Combined sources
    Beta strandi384 – 3874Combined sources
    Beta strandi391 – 3933Combined sources
    Turni408 – 4125Combined sources
    Turni414 – 4174Combined sources
    Turni423 – 4253Combined sources
    Beta strandi433 – 44210Combined sources
    Turni444 – 4463Combined sources
    Helixi447 – 4559Combined sources
    Beta strandi456 – 4583Combined sources
    Beta strandi461 – 47010Combined sources
    Beta strandi472 – 4743Combined sources
    Helixi475 – 4839Combined sources
    Beta strandi489 – 4946Combined sources
    Helixi499 – 50911Combined sources
    Beta strandi512 – 5176Combined sources
    Helixi528 – 53811Combined sources
    Beta strandi543 – 55210Combined sources
    Beta strandi558 – 5614Combined sources
    Helixi570 – 5734Combined sources
    Beta strandi583 – 5864Combined sources
    Helixi587 – 5904Combined sources
    Turni591 – 5944Combined sources
    Helixi604 – 6129Combined sources
    Turni613 – 6153Combined sources
    Beta strandi618 – 62912Combined sources
    Helixi640 – 65415Combined sources
    Turni655 – 6595Combined sources
    Beta strandi662 – 6687Combined sources
    Beta strandi677 – 6815Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8L0V4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni143 – 317175A1Add
    BLAST
    Regioni424 – 596173A2Add
    BLAST

    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_LQWQ01000271.1.

    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_LQWQ01000271.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z86X-ray2.40A/B/C/D58-682[»]
    2Z87X-ray3.00A/B59-682[»]
    ProteinModelPortaliQ8L0V4.
    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: May 11, 2016
    This is version 44 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.