PAPS1_CAVPO
ID PAPS1_CAVPO Reviewed; 624 AA.
AC O54820;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1;
DE Short=PAPS synthase 1;
DE Short=PAPSS 1;
DE AltName: Full=Sulfurylase kinase 1;
DE Short=SK 1;
DE Short=SK1;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4 {ECO:0000250|UniProtKB:O43252};
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25 {ECO:0000250|UniProtKB:O43252};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate synthase;
DE AltName: Full=APS kinase;
DE AltName: Full=Adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenylylsulfate 3'-phosphotransferase;
GN Name=PAPSS1; Synonyms=ATPSK1, PAPSS;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH 2;
RA Venkatachalam K.V., Akita H., Strott C.A.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase
CC activity, which mediates two steps in the sulfate activation pathway.
CC The first step is the transfer of a sulfate group to ATP to yield
CC adenosine 5'-phosphosulfate (APS), and the second step is the transfer
CC of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate
CC (PAPS: activated sulfate donor used by sulfotransferase). In mammals,
CC PAPS is the sole source of sulfate; APS appears to be only an
CC intermediate in the sulfate-activation pathway. Required for normal
CC biosynthesis of sulfated L-selectin ligands in endothelial cells.
CC {ECO:0000250|UniProtKB:O43252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4;
CC Evidence={ECO:0000250|UniProtKB:O43252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000250|UniProtKB:O43252};
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC {ECO:0000250|UniProtKB:O43252}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43252}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AF004875; AAC02266.1; -; mRNA.
DR RefSeq; NP_001166466.1; NM_001172995.1.
DR AlphaFoldDB; O54820; -.
DR SMR; O54820; -.
DR STRING; 10141.ENSCPOP00000010347; -.
DR GeneID; 100135593; -.
DR KEGG; cpoc:100135593; -.
DR CTD; 9061; -.
DR eggNOG; KOG4238; Eukaryota.
DR InParanoid; O54820; -.
DR OrthoDB; 528280at2759; -.
DR BRENDA; 2.7.1.25; 1225.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; ISS:UniProtKB.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; ISS:UniProtKB.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..624
FT /note="Bifunctional 3'-phosphoadenosine 5'-phosphosulfate
FT synthase 1"
FT /id="PRO_0000105958"
FT REGION 1..225
FT /note="Adenylyl-sulfate kinase"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT REGION 234..624
FT /note="Sulfate adenylyltransferase"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 62..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 89..92
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 101
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 106..109
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 132..133
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 171
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 184..185
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 419..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 521..525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60967"
SQ SEQUENCE 624 AA; 70396 MW; BF7461B4D07F2131 CRC64;
MELPGSLCKK AKLGHGAQSW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL
SGAGKTTVSM ALGEHLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG
EIKGFTGIDS EYEKPEAPEL VLKTDACDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP
ENKLHLAKTD AESLPALQIN KVDMQWVQVL AEGWATPLGG FMREREYLQC LHFDCLLDGG
VINLSVPIVL TATEEDKERL DGCTAFALIY EGRRVAILRN PEFFEHRKEE RCARQWGTTC
KSHPYIKMVM EQGDWLIGGD LQVLDRIYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL
RNPVHNGHAL LMQDTHRQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGI
LNPESTVVAI FPSPMMYAGP TGVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYKPT
HGAKVLTMAP GLITLEIVPF RVAAYNKRKK RMDYYDAEHH EDFEFISGTR MRRLAREGQK
PPEGFMAPTA WAVLAEYYKA LEKA
