ID   Q9QYS0_MOUSE            Unreviewed;       621 AA.
AC   Q9QYS0;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   SubName: Full=ATP sulfurylase/APS kinase isoform SK2 {ECO:0000313|EMBL:AAF12760.1};
DE            EC=2.7.1.25 {ECO:0000313|EMBL:AAF12760.1};
DE            EC=2.7.7.4 {ECO:0000313|EMBL:AAF12760.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAF12760.1};
RN   [1] {ECO:0000313|EMBL:AAF12760.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAF12760.1};
RX   PubMed=9671738; DOI=10.1073/pnas.95.15.8681;
RA   Kurima K., Warman M.L., Krishnan S., Domowicz M., Krueger R.C.Jr.,
RA   Deyrup A., Schwartz N.B.;
RT   "A member of a new family of sulfate activating enzymes causes murine
RT   brachymorphism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8681-8685(1998).
RN   [2] {ECO:0000313|EMBL:AAF12760.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAF12760.1};
RX   PubMed=10559207; DOI=10.1074/jbc.274.47.33306;
RA   Kurima K., Singh B., Schwartz N.B.;
RT   "Genomic organization of the mouse and human genes encoding the ATP
RT   sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2.";
RL   J. Biol. Chem. 274:33306-33312(1999).
CC   -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC       {ECO:0000256|ARBA:ARBA00005050}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00009290}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC       family. {ECO:0000256|ARBA:ARBA00007268}.
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DR   EMBL; AH008407; AAF12760.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9QYS0; -.
DR   PeptideAtlas; Q9QYS0; -.
DR   UniPathway; UPA00097; -.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0034033; P:purine nucleoside bisphosphate biosynthetic process; IEA:UniProt.
DR   GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:UniProt.
DR   GO; GO:0034030; P:ribonucleoside bisphosphate biosynthetic process; IEA:UniProt.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02027; APSK; 1.
DR   CDD; cd00517; ATPS; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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   NCBIfam; TIGR00455; apsK; 1.
DR   NCBIfam; TIGR00339; sopT; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF16; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 2; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:AAF12760.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AAF12760.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAF12760.1}.
FT   DOMAIN          218..382
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          390..612
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   621 AA;  70409 MW;  019519DC8E239F68 CRC64;
     MSANFKMNHK RDQQKSTNVV YQAHHVSRNK RGQVVGTRGG FRGCTVWLTG LPGAGKTTIS
     FALEEYLVSH AIPCYSLDGD NVRHGLNKNL GFSAGDREEN IRRIAEVARL FADAGLVCIT
     SFISPFAKDR ENARKIHESA GLPFFEIFVD APLNICESRD VKGLYKRARA GEIKGFTGID
     SDYEKPETPE CVLKTNLSSV SDCVQQVVEL LQEQNIVPHT TIKGIHELFV PENKVDQIRA
     EAETLPSPPI TKLDLQWVQI LSEGWATPLK GFMREKEYLQ TLHFDTLLDG VVPRDGVINM
     SIPIVLPVSA DDKARLEGCS KFALMYEGRR VALLQDPEFY EHRKEERCSR VWGTATAKHP
     HIKMVMESGD WLVGGDLQVL ERIRWDDGLD QYRLTPLELK QKCKDMNADA VYAFQLRNPV
     HNGHALMMQD TRRRLLERGY KHPVLLLHPL GGWTKDDDVP LEWRMKQHTA VLEERVLDPK
     STIVAIFPSP MLYAGPTEVQ WHCRCRMIAG ANFYIVGRDP AGMPHPETKK DLYEPTHGGK
     VLSMAPGLTS VEIIPFRVAA YNKIKKAMDF YDPARHEEFD FISGTRMRKL AREGEDPPDG
     FMAPKAWKVL TDYYRSLEKT N
//