CHS_PASMU
ID CHS_PASMU Reviewed; 965 AA.
AC Q9CMP0; Q6PKM8; Q9AHL6; Q9KJ99;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chondroitin synthase;
DE Short=CS;
DE Includes:
DE RecName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase;
DE EC=2.4.1.175 {ECO:0000250|UniProtKB:Q8L0V4};
DE AltName: Full=UDP-GalNAc transferase;
DE Includes:
DE RecName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase;
DE EC=2.4.1.226 {ECO:0000250|UniProtKB:Q8L0V4};
DE AltName: Full=UDP-GlcUA transferase;
GN Name=fcbD; OrderedLocusNames=PM0775;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serogroup F / P4679;
RX PubMed=10818104; DOI=10.1074/jbc.m003385200;
RA DeAngelis P.L., Padgett-McCue A.J.;
RT "Identification and molecular cloning of a chondroitin synthase from
RT Pasteurella multocida type F.";
RL J. Biol. Chem. 275:24124-24129(2000).
RN [2]
RP SEQUENCE REVISION TO 335-336; 386; 398 AND 692.
RA DeAngelis P.L., Padgett-McCue A.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serogroup F / P4218;
RX PubMed=11230405; DOI=10.1128/jcm.39.3.924-929.2001;
RA Townsend K.M., Boyce J.D., Chung J.Y., Frost A.J., Adler B.;
RT "Genetic organization of Pasteurella multocida cap loci and development of
RT a multiplex capsular PCR typing system.";
RL J. Clin. Microbiol. 39:924-929(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serogroup F / J-4103;
RA Jaglic Z., Bartos M.;
RT "The first detection of Pasteurella multocida serogroup F in rabbits:
RT analysis of serogroup F specific fcbD gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: Glycosyltransferase that catalyzes elongation of chondroitin,
CC a polysaccharide composed of a repeating disaccharide of N-
CC acetylgalactosamine (GalNAc) and glucuronic acid (GlcUA) units, by
CC alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA
CC and UDP-GalNAc to the non-reducing ends of the chondroitin chain. Each
CC chondroitin unit has the composition beta-(1->4)-GlcUA-beta-(1->3)-
CC GalNAc. {ECO:0000250|UniProtKB:Q8L0V4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC Evidence={ECO:0000250|UniProtKB:Q8L0V4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC Evidence={ECO:0000250|UniProtKB:Q8L0V4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226; Evidence={ECO:0000250|UniProtKB:Q8L0V4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC Evidence={ECO:0000250|UniProtKB:Q8L0V4};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8L0V4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CS/HAS
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF195517; AAF97500.2; -; Genomic_DNA.
DR EMBL; AF302467; AAK17921.1; -; Genomic_DNA.
DR EMBL; AY604234; AAT10183.1; -; Genomic_DNA.
DR EMBL; AE004439; AAK02859.1; -; Genomic_DNA.
DR RefSeq; WP_010906847.1; NC_002663.1.
DR AlphaFoldDB; Q9CMP0; -.
DR SMR; Q9CMP0; -.
DR STRING; 272843.PM0775; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; Q9CMP0; -.
DR EnsemblBacteria; AAK02859; AAK02859; PM0775.
DR KEGG; pmu:PM0775; -.
DR PATRIC; fig|272843.6.peg.784; -.
DR HOGENOM; CLU_013018_0_0_6; -.
DR BRENDA; 2.4.1.175; 4558.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 2.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 2.
DR SUPFAM; SSF53448; SSF53448; 2.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Manganese; Membrane; Metal-binding;
KW Multifunctional enzyme; Reference proteome; Repeat; Transferase.
FT CHAIN 1..965
FT /note="Chondroitin synthase"
FT /id="PRO_0000059258"
FT REGION 132..418
FT /note="Galactosaminyltransferase; A1 domain"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT REGION 419..683
FT /note="Glucuronosyltransferase; A2 domain"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 158
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 162
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 189
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 218
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 224
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 240..241
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 362..363
FT /ligand="UDP-N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:67138"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 387
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 442
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 470
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 518..521
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 522
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 582
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 604..605
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT BINDING 632
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8L0V4"
FT CONFLICT 157
FT /note="I -> T (in Ref. 3; AAK17921)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> S (in Ref. 3; AAK17921)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="K -> N (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..643
FT /note="NLDT -> KLGI (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 660..663
FT /note="RVSN -> GINY (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="E -> K (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="N -> D (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="D -> E (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="I -> M (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..701
FT /note="IKIVQR -> LKLIQN (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 706..708
FT /note="VAI -> IAV (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 715..717
FT /note="RLD -> TLN (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 733..740
FT /note="VLIIVLHI -> IFVIILHV (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="S -> P (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 755..762
FT /note="EFHNKNQI -> AFYHKHQV (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="V -> I (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="N -> S (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="K -> E (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="M -> I (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="R -> S (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="L -> C (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="I -> V (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 817..819
FT /note="NHI -> AYM (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="I -> V (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="S -> A (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="N -> H (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="N -> E (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="S -> P (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="N -> K (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="K -> T (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 859..863
FT /note="KTINM -> RSMNV (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="I -> M (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 875..884
FT /note="TLAHDIATIM -> ALPHELLTII (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="L -> S (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="T -> I (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="A -> V (in Ref. 4; AAT10183)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="E -> Q (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
FT CONFLICT 949
FT /note="R -> K (in Ref. 1; AAF97500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 965 AA; 111601 MW; 9C4B2CF80E1A6BD7 CRC64;
MNTLSQAIKA YNSNDYELAL KLFEKSAETY GRKIVEFQII KCKEKLSTNS YVSEDKKNSV
CDSSLDIATQ LLLSNVKKLT LSESEKNSLK NKWKSITGKK SENAEIRKVE LVPKDFPKDL
VLAPLPDHVN DFTWYKNRKK SLGIKPVNKN IGLSIIIPTF NRSRILDITL ACLVNQKTNY
PFEVVVADDG SKENLLTIVQ KYEQKLDIKY VRQKDYGYQL CAVRNLGLRT AKYDFVSILD
CDMAPQQLWV HSYLTELLED NDIVLIGPRK YVDTHNITAE QFLNDPYLIE SLPETATNNN
PSITSKGNIS LDWRLEHFKK TDNLRLCDSP FRYFSCGNVA FSKEWLNKVG WFDEEFNHWG
GEDVEFGYRL FAKGCFFRVI DGGMAYHQEP PGKENETDRE AGKSITLKIV KEKVPYIYRK
LLPIEDSHIH RIPLVSIYIP AYNCANYIQR CVDSALNQTV VDLEVCICND GSTDNTLEVI
NKLYGNNPRV RIMSKPNGGI ASASNAAVSF AKGYYIGQLD SDDYLEPDAV ELCLKEFLKD
KTLACVYTTN RNVNPDGSLI ANGYNWPEFS REKLTTAMIA HHFRMFTIRA WHLTDGFNEK
IENAVDYDMF LKLSEVGKFK HLNKICYNRV LHGDNTSIKN LDTQKKNHFV VVNQSLNRQR
VSNYNYDEFD NLDESRKYIF NKTADYQEEI DILKDIKIVQ RKDAKVAISI FYPNRLDGLV
KKLNNIIEYN KNVLIIVLHI DKNHLTSDIK KEILEFHNKN QINILLNNDV SYYTNNRLIK
TKAHLSNMNK LRQLNLNLEY IIFDNHDSLF IKNDSYNHIK KYDIGMNFSS LTNDWINKIN
AHSPFKNLIK KYFNDNDLKT INMKGASQGM FIKYTLAHDI ATIMKEVITL CQSTDSVPEY
NTEDIWFQFA LLILEKKTGH VFNKTSTLTY MPWERKLQWT NEQIESAKRG ENIPVNKFII
NSITL
