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Protein

Chondroitin synthase

Gene

kfoC

Organism
Escherichia coli
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Glycosyltransferase that catalyzes elongation of chondroitin, a polysaccharide composed of a repeating disaccharide of N-acetylgalactosamine (GalNAc) and glucuronic acid (GlcUA) units, by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Each chondroitin unit has the composition beta-(1->4)-GlcUA-beta-(1->3)-GalNAc.1 Publication

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.1 Publication
UDP-N-acetyl-alpha-D-galactosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine.1 Publication
UDP-N-acetyl-alpha-D-galactosamine + [protein]-3-O-(beta-D-GlcA-(1->3)-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3))(n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-((beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3))(n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine.1 Publication

Cofactori

Mn2+2 PublicationsNote: Binds 2 Mn2+ ions per subunit.1 Publication

Kineticsi

  1. KM=3.44 µM for UDP-GlcUA1 Publication
  2. KM=31.6 µM for UDP-GalNAc1 Publication

    pH dependencei

    Optimum pH is 7-7.5.1 Publication

    Temperature dependencei

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei157UDP-N-acetyl-alpha-D-galactosamine; via carbonyl oxygen1 Publication1
    Binding sitei161UDP-N-acetyl-alpha-D-galactosamine1 Publication1
    Binding sitei188UDP-N-acetyl-alpha-D-galactosamine1 Publication1
    Binding sitei217UDP-N-acetyl-alpha-D-galactosamine1 Publication1
    Binding sitei223UDP-N-acetyl-alpha-D-galactosamine1 Publication1
    Metal bindingi241Manganese 11 Publication1
    Metal bindingi386Manganese 1; via tele nitrogen1 Publication1
    Binding sitei441UDP-alpha-D-glucuronate; via amide nitrogen1 Publication1
    Binding sitei469UDP-alpha-D-glucuronate1 Publication1
    Metal bindingi521Manganese 21 Publication1
    Binding sitei581UDP-alpha-D-glucuronate; via tele nitrogen1 Publication1
    Metal bindingi631Manganese 2; via tele nitrogen1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosyltransferase, Multifunctional enzyme, Transferase
    LigandManganese, Metal-binding

    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:2.4.1.1751 Publication)
    Alternative name(s):
    UDP-GalNAc transferase
    N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC:2.4.1.2261 Publication)
    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
    Regioni130 – 417Galactosaminyltransferase; A1 domain1 PublicationAdd BLAST288
    Regioni239 – 240UDP-N-acetyl-alpha-D-galactosamine binding1 Publication2
    Regioni361 – 362UDP-N-acetyl-alpha-D-galactosamine binding1 Publication2
    Regioni418 – 682Glucuronosyltransferase; A2 domain1 PublicationAdd BLAST265
    Regioni517 – 520UDP-alpha-D-glucuronate binding1 Publication4
    Regioni603 – 604UDP-alpha-D-glucuronate binding1 Publication2

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    KOiK13500

    Family and domain databases

    Gene3Di3.90.550.10, 3 hits
    InterProiView protein in InterPro
    IPR001173 Glyco_trans_2-like
    IPR029044 Nucleotide-diphossugar_trans
    PfamiView protein in Pfam
    PF00535 Glycos_transf_2, 2 hits
    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_NOEF01000002.1

    Genome annotation databases

    KEGGiag:BAC00523

    Similar proteinsi

    Entry informationi

    Entry nameiCHS_ECOLX
    AccessioniPrimary (citable) accession number: Q8L0V4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: October 1, 2002
    Last modified: April 25, 2018
    This is version 50 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure
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    Main funding by: National Institutes of Health