ID A0A0H5SCJ0_BRUMA Unreviewed; 859 AA.
AC A0A0H5SCJ0; A0A0K0J960;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN Name=bma-hst-1 {ECO:0000313|WormBase:Bm3182};
GN ORFNames=Bm3182 {ECO:0000313|WormBase:Bm3182}, BM_Bm3182
GN {ECO:0000313|EMBL:CRZ25811.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ25811.1};
RN [1] {ECO:0000313|EMBL:CRZ25811.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25811.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ25811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25811.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm3182.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2022) to UniProtKB.
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; LN857014; CRZ25811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5SCJ0; -.
DR EnsemblMetazoa; Bm3182.1; Bm3182.1; WBGene00223443.
DR WBParaSite; Bm3182.1; Bm3182.1; WBGene00223443.
DR WormBase; Bm3182; BM35251; WBGene00223443; Bma-hst-1.
DR OMA; GRQYPTM; -.
DR OrthoDB; 2913264at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000006672; 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: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; 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:UP000006672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..493
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 586..828
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 594
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 690
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 808..812
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 794..803
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 859 AA; 99601 MW; BB5ECC06A16D4E5E CRC64;
MLTLPTRRII FWLKLAIIIT CISFIFLFTH LAEITEKPHY RYPAQHIPPY HCPLSNKTGT
TYKHHGFVRN KTNFLTDGKV LVFVETLYSK LGKQIINILD ALKIPRKVET LTKNLPLLTT
AKRGRFSIII VENYYKYLNL LSWNRQLLDK YCREYNVGII SFIGNRPNSY INAKVKGSQL
TIHTQQRAVN LRFNERSRVN FISKPGAVLQ APEPDKNDWI LFDIISGYEG IVLADDIFGE
ERASVILDDG SEDGIEKILF GHNFTHWINK LAFLDSLRYM RESLMYDDLE RFVQIDIDDI
FVGTSGTRMT KVDADALLQS QFRLRRDITN FTYSLGFSGY YFRNGDSLED KGDERLIEIG
KHFLWFPHMW KHNHAHEHNQ TYLEAIMTQN KLFAQSMALH VSSGYAVSPQ HAGVYPVHEA
LYNSWQLIWN ITVTSTEEYP HFRPASARRG FVHRNISVLP RQTCGLYTHT QFFHSYPDGF
TKLLSNIEGG DLFFTIVINP FSIFMTHQQN YANDRLGIFS FERVINFIKC WTNLRLRWVE
PVRMASAYFA RYAAEKVPVW SNPCDDPRHA KILPQPFNCS EMPLPNMLVV GPQKTGSTAL
ATFLNLHPNF SSNDPVPSSF EELQFFGGPN YARGLHWYMD QFRSKIDHLI VFEKSATYFD
NPDAPRTSFA LLPKAKIVII LLDPAARAYS WYHHMRAHND TTAMTHELDQ ILDANVSSVL
LRRLRNRCIS PGRYTHHLEH WLDYYPSTQI HLVDGEQLRT DPVTAITNLV DTLHAPKFAF
SDLIKFDDKK GFFCSYINGT KRCLGTGKGR KYEPLDEKLR EKLDLIFRDD NIALHKLLLR
NDLPIPKWLQ NQLSKTNFT
//
