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Database: UniProt
Entry: A0A091MJI5_9PASS
LinkDB: A0A091MJI5_9PASS
Original site: A0A091MJI5_9PASS 
ID   A0A091MJI5_9PASS        Unreviewed;       873 AA.
AC   A0A091MJI5;
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=N310_06301 {ECO:0000313|EMBL:KFP73947.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP73947.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP73947.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP73947.1};
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; KK827569; KFP73947.1; -; Genomic_DNA.
DR   RefSeq; XP_009082805.1; XM_009084557.1.
DR   AlphaFoldDB; A0A091MJI5; -.
DR   GeneID; 103811573; -.
DR   KEGG; achl:103811573; -.
DR   CTD; 9348; -.
DR   OrthoDB; 2913264at2759; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000053537; 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:SF29; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 3; 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:UP000053537};
KW   Transferase {ECO:0000313|EMBL:KFP73947.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..506
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          596..844
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        605
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         703
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         808
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         824..828
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        809..819
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   873 AA;  100837 MW;  0BBD64BFC9AC55EA CRC64;
     MSFILKLHRH FQRTVILLAT FCMVSIVISA YYLYNGYKQE NELPEISSEV ECGDPQLLPY
     KLMEMKTVKP IDPLRTDLVV LVFVESQYST LGQDIITILE SSRFQFHIEI APGKGDLPVL
     IDKNRGKYAL IVYENILKYV NMDSWNRGLL DKYCIEYGVG VIGFHKGSEN SLQSFQLKGF
     PFHVHSNLGI KDCCINPHSP LLHVTKSSKL EKGPLLGNDW AVFQINHTAY QPVIFAKVKA
     PENLSPPAAL GALYATVIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKKLRLS
     LDRYILVDID DIFVGKEGTR MNTNDVQALL DTQNLLRAQI TNFTFNLGYS GKFYHTGTEE
     EDEGDDLLLR SVDEFWWFPH MWSHMQPHLF HNESSLVEQM ILNKKFALEH GIPTDLGYAV
     APHHSGVYPV HVQLYDAWKK VWNIRVTSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF
     THTIFYKEYP GGPKELDKSI QGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF
     VHTWTNLKLQ TLPPVQLAHK YFELFPEQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV
     VGPQKTGTTA LYLFLIMHPS IISNSPSPKT FEEVQFFNRN NYHRGIDWYM DFFPTPSNIT
     TDLLFEKSAN YFHSEEAPKR AASLIPKAKI ITILIDPSDR AYSWYQHQRS HEDPAALKFS
     FYQVITAGPR APAELRALQK RCLAPGWYAT HIERWLTYFP PYQLLIIDGQ QLRTDPSTVM
     DEVQKFLGVS PHYNYSEALT FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSECRAFLS
     SYYRDHNVEL SKLLHKLGQP LPSWLRQELQ KVR
//
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