ID   A0A0C2D2F1_9BILA        Unreviewed;       719 AA.
AC   A0A0C2D2F1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE            EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN   ORFNames=ANCDUO_13608 {ECO:0000313|EMBL:KIH56212.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH56212.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH56212.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH56212.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005093}.
CC   -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004841}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000256|ARBA:ARBA00010420}.
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DR   EMBL; KN736080; KIH56212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2D2F1; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF56; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   Pfam; PF12062; HSNSD; 2.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Transferase {ECO:0000313|EMBL:KIH56212.1}.
FT   DOMAIN          105..338
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          337..385
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          453..660
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        462
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         555
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         672..676
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        658..667
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   719 AA;  83229 MW;  854462970085D7BE CRC64;
     MRLFRYREED VTQSLECLWH VIWLVPGKAA DFIMLPYCSR RLLKSLKFVI ALTMLFSVTL
     IYKVSFRPDI AVKRYPPQQL PRYECPCNTS SVPNRESPYA NQNLTEHRAL ILLESAYSRH
     GRLLQQILTA SKYPFKAETF SKNLPLLTTA TRGRYAIIII ENYYKYLNMA RWNRQLLDKY
     CVDYNVPLIS FLSTRPNTTY QKVKIKGSKL HFWQNQEVLS LKVAESDIHR ISRIGNERTD
     VNTQEWILFE ESPAVSTVIS ARDSFGRPRA AVVHDRGEED NVKRILFGHN VTDWTIKMTF
     LDVLWYTTGG RVGWSLDRYV QIDVDDIFVG ARGTRMNMRL PVKYPYAIAP QHDGVYPVHS
     ELYKAWKKVS IFMTHQQNFA HDRLALYTFD NLVRFIQCWT NIRLLWQSPV ESAKKYFSLM
     PQERLPVWSN PCNDPRHKAI LPPSLNCSNL TLPNTLIVGP QKTGSTALAT FLSLHPNVST
     NAPIPDSFEE LQFFGGANYH NGIEWYTRQF TRAHVVYDKS ATYFDNANAA RDAFALVPDA
     KIVVILYDPA RRAYSWYQHI LAHNDSVAVA AGSMDVILNA ETPQLRKIKQ RCISGGRYTH
     HLDRWLEHYP MSNLILVDGE RLREEPAIVM TELTEKLGLP YFDYSKAVRY SSSKRFFCQV
     IDGKTKCLGR GKGRVYPPMP PELWARLNNI FLQDNTALHK FLVKNHLPVP KWLRSLLEG
//