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Database: UniProt
Entry: A0A091M842_CARIC
LinkDB: A0A091M842_CARIC
Original site: A0A091M842_CARIC 
ID   A0A091M842_CARIC        Unreviewed;       855 AA.
AC   A0A091M842;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=N322_03735 {ECO:0000313|EMBL:KFP67973.1};
OS   Cariama cristata (Red-legged seriema).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX   NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP67973.1, ECO:0000313|Proteomes:UP000054116};
RN   [1] {ECO:0000313|EMBL:KFP67973.1, ECO:0000313|Proteomes:UP000054116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP67973.1};
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}.
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DR   EMBL; KK525488; KFP67973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091M842; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   Proteomes; UP000054116; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW   Transferase {ECO:0000313|EMBL:KFP67973.1}.
FT   DOMAIN          58..488
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          578..831
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        587
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         685
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         790
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         806..810
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        791..801
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP67973.1"
FT   NON_TER         855
FT                   /evidence="ECO:0000313|EMBL:KFP67973.1"
SQ   SEQUENCE   855 AA;  98417 MW;  52BCC4BE67D699C3 CRC64;
     LFVFCLLSVF VSAYYLYGWK RGLEPSGDVV GPDCDEPKVA PSRLLPLKTL KVVDSSRTDP
     LVLVFVESLY SQLGQEIVAI LESSRFKYRT EIAPGKGDMP TLTDKDRGRF ALIIYENILK
     YVNLDAWNRE LLDKYCVEYG VGIIGFFKAN ENSLLSAQLK GFPLFLHSNL ALKDCSINPK
     SPLLYITRPS EVEKGVLPGE DWTVFQSNHS TYEPVLLAKT KSAESIPHMS VDAALHTTVM
     QDLGLHDGIQ RVLFGNNLNF WLHKLVFVDS VSFLTGKRLS LPLDRYILVD IDDIFVGKEG
     TRMKVEDVKA LFDTQNELRT HIPNFTFNLG YSGKFFHTGT DAEDEGDDLL LSYVREFWWF
     PHMWSHMQPH LFHNQSVLAE QMTLNKKFAV EHGIPTDMGY AVAPHHSGVY PVHVQLYEAW
     KQVWSIKVTS TEEYPHLKPA RYRRGFIHNG IMVLPRQTCG LFTHTIFYNE YPGGSSELDK
     IINGGELFLT VLLNPISIFM THLSNYGNDR LGLYTFKHLV RFLNSWTNLK LQTLPPVQLA
     QKYFQIFSEE KDPLWQDPCE DKRHKDIWSK EKTCDRFPKL LIIGPQKTGT TALYLFLGMH
     PDLSSNYPSS ETFEEIQFFN GHNYHKGIDW YMEFFPIPSN TTSDFYFEKS ANYFDSEVAP
     RRAAALLSKA KVITILINPA DRAYSWYQHQ RAHDDPVALK YTFHEVITAG PEAAPKLRTL
     QNRCLVPGWY ATHIERWLNS YHANQILVLD GKLLRTEPAK VMETVQKFLG VTNFIDYHKT
     LAFDPKKGFW CQLLDGGKTK CLGKSKGRKY PEMDSDSRAF LRDYYRDHNI ELSKLLYKMG
     QTLPTWLREE LQSTR
//
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