ID A0A087V796_BALRE Unreviewed; 872 AA.
AC A0A087V796;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 {ECO:0000256|ARBA:ARBA00039538};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1 {ECO:0000256|ARBA:ARBA00042929};
DE Flags: Fragment;
GN ORFNames=N312_04968 {ECO:0000313|EMBL:KFO08488.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO08488.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO08488.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO08488.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00036125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21981;
CC Evidence={ECO:0000256|ARBA:ARBA00036125};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004841}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00037848}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00037848}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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; KL482563; KFO08488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087V796; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000053309; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:SF30; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 1; 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:UP000053309};
KW Transferase {ECO:0000313|EMBL:KFO08488.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..505
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 595..848
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 604
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 702
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 807
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 823..827
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 808..818
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO08488.1"
FT NON_TER 872
FT /evidence="ECO:0000313|EMBL:KFO08488.1"
SQ SEQUENCE 872 AA; 100302 MW; 53190A4A058A25A1 CRC64;
RARRGIRQLS PQVVLLLLFV FCLLSVFISA YYLYGWKRGL EPSGDVAGPD CDEPKVAPSR
LLPLKALKVA DSSRTDPLVL VFVESLYSQL GQEIVAILES SRFKYRTEIA PGKGDMPTLT
DKDRGRFALI IYENILKYVN LDAWNRELLD KYCVEYGVGI IGFFKANENS LLSAQLKGFP
LFLHSNLALK DCSINPKSPL LYITRPSEVE KGVLPGEDWT VFQSNHSTYE PVLLAKTKSA
ESIPHMSVDA ALHTTVMQDL GLHDGIQRVL FGNNLNFWLH KLVFVDSVSF LTGKRLSLPL
DRYILVDIDD IFVGKEGTRM KVEDVKALFD TQNELRTHIP NFTFNLGYSG KFFHTGTDAE
DEGDDLLLSY VREFWWFPHM WSHMQPHLFH NQSVLAEQMT LNKKFAVEHG IPTDMGYAVA
PHHSGVYPVH VQLYEAWKQV WSIKVTSTEE YPHLKPARYR RGFIHNGIMV LPRQTCGLFT
HTIFYNEYPG GSSELDKIIN GGELFLTVLL NPISIFMTHL SNYGNDRLGL YTFKHLVRFL
NSWTNLKLQT LPPVQLAQKY FQIFSEEKDP LWQDPCEDKR HKDIWSKEKT CDRFPKLLII
GPQKTGTTAL YLFLGMHPDL SSNYPSSETF EEIQFFNGHN YHKGIDWYME FFPIPSNTTS
DFYFEKSANY FDSEVAPRRA AALLSKAKVI TILINPADRA YSWYQHQRAH DDPVALKYTF
HEVITAGPEA APKLRTLQNR CLVPGWYATH IERWLNSYHA NQILVLDGKL LRTEPAKVME
TVQKFLGVTN FIDYHKTLAF DPKKGFWCQL LDGGKTKCLG KSKGRKYPEM DSDSRAFLRD
YYRDHNIELS KLLYKMGQTL PTWLREELQS TR
//
