Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chondroitin synthase

Gene

fcbD

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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.By similarity

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.By similarity
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.By similarity
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.By similarity

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei158UDP-N-acetyl-alpha-D-galactosamine; via carbonyl oxygenBy similarity1
Binding sitei162UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei189UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei218UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Binding sitei224UDP-N-acetyl-alpha-D-galactosamineBy similarity1
Metal bindingi242Manganese 1By similarity1
Metal bindingi387Manganese 1; via tele nitrogenBy similarity1
Binding sitei442UDP-alpha-D-glucuronate; via amide nitrogenBy similarity1
Binding sitei470UDP-alpha-D-glucuronateBy similarity1
Metal bindingi522Manganese 2By similarity1
Binding sitei582UDP-alpha-D-glucuronate; via tele nitrogenBy similarity1
Metal bindingi632Manganese 2; via tele nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciPMUL272843:G1FZ8-815-MONOMER
BRENDAi2.4.1.175 4558

Protein family/group databases

CAZyiGT2 Glycosyltransferase Family 2

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin synthase
Short name:
CS
Including the following 2 domains:
Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase (EC:2.4.1.175By similarity)
Alternative name(s):
UDP-GalNAc transferase
N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC:2.4.1.226By similarity)
Alternative name(s):
UDP-GlcUA transferase
Gene namesi
Name:fcbD
Ordered Locus Names:PM0775
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
Proteomesi
  • UP000000809 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000592581 – 965Chondroitin synthaseAdd BLAST965

Interactioni

Protein-protein interaction databases

STRINGi272843.PM0775

Structurei

3D structure databases

ProteinModelPortaliQ9CMP0
SMRiQ9CMP0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 418Galactosaminyltransferase; A1 domainBy similarityAdd BLAST287
Regioni240 – 241UDP-N-acetyl-alpha-D-galactosamine bindingBy similarity2
Regioni362 – 363UDP-N-acetyl-alpha-D-galactosamine bindingBy similarity2
Regioni419 – 683Glucuronosyltransferase; A2 domainBy similarityAdd BLAST265
Regioni518 – 521UDP-alpha-D-glucuronate bindingBy similarity4
Regioni604 – 605UDP-alpha-D-glucuronate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0726 LUCA
HOGENOMiHOG000154388
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.

Q9CMP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTLSQAIKA YNSNDYELAL KLFEKSAETY GRKIVEFQII KCKEKLSTNS
60 70 80 90 100
YVSEDKKNSV CDSSLDIATQ LLLSNVKKLT LSESEKNSLK NKWKSITGKK
110 120 130 140 150
SENAEIRKVE LVPKDFPKDL VLAPLPDHVN DFTWYKNRKK SLGIKPVNKN
160 170 180 190 200
IGLSIIIPTF NRSRILDITL ACLVNQKTNY PFEVVVADDG SKENLLTIVQ
210 220 230 240 250
KYEQKLDIKY VRQKDYGYQL CAVRNLGLRT AKYDFVSILD CDMAPQQLWV
260 270 280 290 300
HSYLTELLED NDIVLIGPRK YVDTHNITAE QFLNDPYLIE SLPETATNNN
310 320 330 340 350
PSITSKGNIS LDWRLEHFKK TDNLRLCDSP FRYFSCGNVA FSKEWLNKVG
360 370 380 390 400
WFDEEFNHWG GEDVEFGYRL FAKGCFFRVI DGGMAYHQEP PGKENETDRE
410 420 430 440 450
AGKSITLKIV KEKVPYIYRK LLPIEDSHIH RIPLVSIYIP AYNCANYIQR
460 470 480 490 500
CVDSALNQTV VDLEVCICND GSTDNTLEVI NKLYGNNPRV RIMSKPNGGI
510 520 530 540 550
ASASNAAVSF AKGYYIGQLD SDDYLEPDAV ELCLKEFLKD KTLACVYTTN
560 570 580 590 600
RNVNPDGSLI ANGYNWPEFS REKLTTAMIA HHFRMFTIRA WHLTDGFNEK
610 620 630 640 650
IENAVDYDMF LKLSEVGKFK HLNKICYNRV LHGDNTSIKN LDTQKKNHFV
660 670 680 690 700
VVNQSLNRQR VSNYNYDEFD NLDESRKYIF NKTADYQEEI DILKDIKIVQ
710 720 730 740 750
RKDAKVAISI FYPNRLDGLV KKLNNIIEYN KNVLIIVLHI DKNHLTSDIK
760 770 780 790 800
KEILEFHNKN QINILLNNDV SYYTNNRLIK TKAHLSNMNK LRQLNLNLEY
810 820 830 840 850
IIFDNHDSLF IKNDSYNHIK KYDIGMNFSS LTNDWINKIN AHSPFKNLIK
860 870 880 890 900
KYFNDNDLKT INMKGASQGM FIKYTLAHDI ATIMKEVITL CQSTDSVPEY
910 920 930 940 950
NTEDIWFQFA LLILEKKTGH VFNKTSTLTY MPWERKLQWT NEQIESAKRG
960
ENIPVNKFII NSITL
Length:965
Mass (Da):111,601
Last modified:June 1, 2001 - v1
Checksum:i9C4B2CF80E1A6BD7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti157I → T in AAK17921 (PubMed:11230405).Curated1
Sequence conflicti170L → S in AAK17921 (PubMed:11230405).Curated1
Sequence conflicti600K → N in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti640 – 643NLDT → KLGI in AAF97500 (PubMed:10818104).Curated4
Sequence conflicti660 – 663RVSN → GINY in AAF97500 (PubMed:10818104).Curated4
Sequence conflicti668E → K in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti671N → D in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti685D → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti690I → M in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti696 – 701IKIVQR → LKLIQN in AAF97500 (PubMed:10818104).Curated6
Sequence conflicti706 – 708VAI → IAV in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti715 – 717RLD → TLN in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti733 – 740VLIIVLHI → IFVIILHV in AAF97500 (PubMed:10818104).Curated8
Sequence conflicti747S → P in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti755 – 762EFHNKNQI → AFYHKHQV in AAF97500 (PubMed:10818104).Curated8
Sequence conflicti770V → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti775N → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti782K → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti788M → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti792R → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti798L → C in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti811I → V in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti817 – 819NHI → AYM in AAF97500 (PubMed:10818104).Curated3
Sequence conflicti824I → V in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti830S → A in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti833N → H in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti837N → E in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti843S → P in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti847N → K in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti851K → T in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti859 – 863KTINM → RSMNV in AAF97500 (PubMed:10818104).Curated5
Sequence conflicti872I → M in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti875 – 884TLAHDIATIM → ALPHELLTII in AAF97500 (PubMed:10818104).Curated10
Sequence conflicti890L → S in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti894T → I in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti910A → V in AAT10183 (Ref. 4) Curated1
Sequence conflicti945E → Q in AAF97500 (PubMed:10818104).Curated1
Sequence conflicti949R → K in AAF97500 (PubMed:10818104).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195517 Genomic DNA Translation: AAF97500.2
AF302467 Genomic DNA Translation: AAK17921.1
AY604234 Genomic DNA Translation: AAT10183.1
AE004439 Genomic DNA Translation: AAK02859.1
RefSeqiWP_010906847.1, NC_002663.1

Genome annotation databases

EnsemblBacteriaiAAK02859; AAK02859; PM0775
KEGGipmu:PM0775
PATRICifig|272843.6.peg.784

Similar proteinsi

Entry informationi

Entry nameiCHS_PASMU
AccessioniPrimary (citable) accession number: Q9CMP0
Secondary accession number(s): Q6PKM8, Q9AHL6, Q9KJ99
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: April 25, 2018
This is version 83 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health