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Database: UniProt
Entry: A0A093D1K7_TAUER
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ID   A0A093D1K7_TAUER        Unreviewed;       879 AA.
AC   A0A093D1K7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE            EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN   ORFNames=N340_09193 {ECO:0000313|EMBL:KFV20633.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV20633.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV20633.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV20633.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL476013; KFV20633.1; -; Genomic_DNA.
DR   RefSeq; XP_009989121.1; XM_009990819.1.
DR   AlphaFoldDB; A0A093D1K7; -.
DR   GeneID; 104382789; -.
DR   KEGG; teo:104382789; -.
DR   CTD; 8509; -.
DR   OrthoDB; 2913264at2759; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000053661; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019213; F:deacetylase activity; IEA:UniProt.
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:SF53; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 2; 1.
DR   PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR   Pfam; PF12062; HSNSD; 1.
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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW   Transferase {ECO:0000313|EMBL:KFV20633.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..510
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          600..849
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        609
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         707
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         812
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         828..832
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        813..823
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   879 AA;  101396 MW;  82A906F691B0A2F8 CRC64;
     MIQLWKVVRH VRQLELHRLI LLLIAFSLIS MCILAYYVTN SPKIKEPPPL PFSDCSNQHR
     ILIPPQASWR LTKSVDTSRT DPVVLVFVES IYSQLGQEIV AILESSRFKY RTEIAPGKGD
     MPTLTDKDRG RYALIIYENI LKYVNLDAWN RELLDKYCVE YGVGIIGFFK ANENSLLSAQ
     LKGFPLFLHS NLGLRDYHIN PSAPLLYVTR ANEVEQGPLP GDDWTVFQSN HSTYEPVLLA
     STKSSESIPH LATHKALHAT VVQDLGLHDG IQRVLFGNNL NFWLHKLIFV DAIAYLTGKR
     LCLTLDRYIL VDIDDIFVGK EGTRMKVSDV EALLSTQNKL RTLVPNFTFN LGFSGKFYHT
     GTDEEDEGDD MLLKHRKEFW WFPHMWSHMQ PHLFHNVTVL AEQMKLNKQF AVEHGIPTDL
     GYAVAPHHSG VYPVHTQLYE AWKSVWSIQV TSTEEYPHLR PARYRRGFIH NGIMVLPRQT
     CGLFTHTIFY NEYPGGSKEL DKSIRGGELF LTVLLNPISI FMTHLSNYGN DRLGLYTFES
     LVKFVQCWTN LRLQTLPPVQ LAKKYFEIFP QEKNPLWQNP CDDKRHKDIW SKEKTCDRLP
     KFLIVGPQKT GTTAVHFFLT MHPAVTSNFP SPSTFEEIQF FNGPNYHKGI DWYMEFFPIP
     SNASTDFMFE KSANYFDTEV VPKRGAALLP RAKIITVLIN PADRAYSWYQ HQRAHNDPVA
     LNYTFYQVIS AKSQAPQELR NLQSRCLLPG WYSAHLERWL TYYPSGQLLI VDGQELRHNP
     AAVMDNIQKF LGVTPLFNYT QALRFDEVKG FWCQLLDGGK TKCLGKSKGR KYPDMDSSSR
     LFLRGFYREH NIELSKLMNR LGQPLPTWLR EELQNSSWS
//
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