ID A0A0M9A1I4_9HYME Unreviewed; 481 AA.
AC A0A0M9A1I4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN ORFNames=WN51_12174 {ECO:0000313|EMBL:KOX75430.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX75430.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX75430.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX75430.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX75430.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC {ECO:0000256|RuleBase:RU364122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140604; Evidence={ECO:0000256|RuleBase:RU364122};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364122}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU364122}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC {ECO:0000256|ARBA:ARBA00010109, ECO:0000256|RuleBase:RU364122}.
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; KQ435762; KOX75430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A1I4; -.
DR STRING; 166423.A0A0M9A1I4; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR PANTHER; PTHR12812:SF0; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU364122};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW Transferase {ECO:0000256|RuleBase:RU364122, ECO:0000313|EMBL:KOX75430.1};
KW Transmembrane {ECO:0000256|RuleBase:RU364122};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364122}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364122"
SQ SEQUENCE 481 AA; 55044 MW; 75046D357A9C8463 CRC64;
MGRRSSEEGV SELSVLVEDD LCERSATMES RARRTRLRSV VGICLFLALT GIIYLGYFCP
DHVCALTSRE IKESVRLSEG LSAGPGSGLS SVSVEFDKNG LLSVHPAFRL HSIQGSLGYD
DVFTNDTFQF DINGHDVIVF LHIQKTGGTL FGKHLVRDLD LQRPCSCQRR RKRCFCFRPN
RNENWLFSRY STGWKCGLHA DWTELTSCVD TELNKIEGDG IKRRYFYITI IRDPVARYLS
EFRHVQRGAT WRGARHWCGG IQANIPQCYP GSSWQGVSLE QFMACPYNLA SNRQTRMLAD
LSIVGCYNST LSSLERDRLM LASAKHNLQF MPFFMLTEYQ KVGQYSFEET FGMRFAVAFE
QHNATLSAAT MATLSAEQLD AVRRLNRLDL ELYDFAKNLA FQRFKRLRDR DPYFVQRFQH
LGELPSRQSA TEFNWDSVIE DTTDLTTKKI ITKQYANALF SRIFIDCVND PQTSLVFSEN
A
//