NDST_CAEBR
ID NDST_CAEBR Reviewed; 859 AA.
AC Q60V90; A8XW41;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1;
DE EC=2.8.2.8;
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase 1;
DE EC=3.-.-.-;
DE Includes:
DE RecName: Full=Heparan sulfate N-sulfotransferase 1;
DE EC=2.8.2.-;
GN Name=hst-1; ORFNames=CBG19653;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
CC deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
CC glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
CC disaccharide repeating sugar backbone to make N-sulfated heparosan, a
CC prerequisite substrate for later modifications in heparin biosynthesis
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140572; EC=2.8.2.8;
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; HE600903; CAP36860.2; -; Genomic_DNA.
DR AlphaFoldDB; Q60V90; -.
DR SMR; Q60V90; -.
DR STRING; 6238.CBG19653; -.
DR WormBase; CBG19653; CBP46453; WBGene00038831; Cbr-hst-1.
DR eggNOG; KOG3703; Eukaryota.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; Q60V90; -.
DR OMA; EMHLNYA; -.
DR OrthoDB; 388292at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605; PTHR10605; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Multifunctional enzyme; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..859
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 1"
FT /id="PRO_0000225663"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..859
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..575
FT /note="Heparan sulfate N-deacetylase 1"
FT REGION 576..859
FT /note="Heparan sulfate N-sulfotransferase 1"
FT ACT_SITE 593
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 593..597
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 810..814
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 796..805
FT /evidence="ECO:0000250"
SQ SEQUENCE 859 AA; 100178 MW; 56D9CD5DA5B886F2 CRC64;
MIITPYLNPR LVKPLKWLAI IILLYFLYFS LFSINKKPGK PRKPPKAVEN YTCPFEKADF
SNFKDKKLEF HKNNGTDPKI LVILDSLFSR HGKSIIQILN SQKFAFKAEA ISKNLPVLTS
AKRGKYSLII VENYYKYLNM ARWNRQLLDK YCKEYRVPLF SFIASKPNDQ LKRIRIKGSS
LWMWQNQRIN RLTVSPSPIH KISKIGAYRN LTTQESDWIL FEISENFESI LTGTVKNGYE
RAVVLRDLGR EDGVEKVIFG RNLTDFQIKI TFLDALWWAM GDEKLFGLDR FVQVDIDDVF
VGAQSTRIVE EDVRHLISAQ NHFRNFIENF KFLLGFSGSY FRNGDDFEDR GDEILIENAE
KFVWFPHMWR HNHAHEHNFT YLESIMVQNR LFAQNMHLPI DYPYAIAPQH DGVFPVHEQM
YEAWKKIWNV TVTATEEYPH LKPATGRKGF IHSGIHVLPR QTCGLYTHTQ FFDEYPEGFQ
KVIKSIQGGD LFFTILLNPI SIFMTHQQNY AHDRLALYTF ENLFRFLNCW TNIRLKWQSP
VESAKMYFEK FPEERIPLWT NPCSDPRHQA ILPPSMSCSK KSLPDLLIIG PQKTGSTALA
SFLALHPNVS QNMEIPGSFE EIQFFSGQNY LKGVEWYMSK FPNETTVIFE KSATYFDNPS
AARQAAAMVP HAKLVIILQN PTQRAYSWFQ SLFQHLIAHK DPIAMSSESL DVILNSTSSE
SAKFKIRQRC LSGGRYVHHL DKWLEHFSLQ QIQFIDSDEL RKEPAKVLSS LSKWLDLPEF
PFETHIRFSP SKGFHCRLIN GKTECLGESK GRKYSEMSQE LRQKLDGIFA LDNSALFKFL
RKNRLKIPDW LEEAVRIRV
