ID   A0A2K5L8P1_CERAT        Unreviewed;       580 AA.
AC   A0A2K5L8P1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=3'-phosphoadenosine 5'-phosphosulfate synthase 1 {ECO:0000313|Ensembl:ENSCATP00000009314.1};
GN   Name=PAPSS1 {ECO:0000313|Ensembl:ENSCATP00000009314.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000009314.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000009314.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A2K5L8P1; -.
DR   Ensembl; ENSCATT00000032814.1; ENSCATP00000009314.1; ENSCATG00000028277.1.
DR   GeneTree; ENSGT00390000009613; -.
DR   OMA; LVYEGCR; -.
DR   UniPathway; UPA00097; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000028277; Expressed in bone marrow and 12 other cell types or tissues.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
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; 2.
DR   Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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; TIGR00339; sopT; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF17; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 1; 1.
DR   Pfam; PF01583; APS_kinase; 2.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          189..341
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          350..573
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   580 AA;  65830 MW;  6B7779E1DFE49D05 CRC64;
     MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL
     SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF
     ADAGLVCITS FISPYTQVCG FTGIDSEYEK PEAPELVLKT DSCDVNDCVQ QVVELLQERD
     IVPVDASYEV KELYVPENKL HLAKTDAETL PALKINKVDM QWVQVLAEGW ATPLNGFMRE
     REYLQCLHFD CLLDGGVINL SVPIVLTATH EDKERLDGCT AFALMYEGRR VAILRNPEFF
     EHRKEERCAR QWGTTCKNHP YIKMVMEQGD WLIGGDLQVL DRVYWNDGLD QYRLTPTELK
     QKFKDMNADA VFAFQLRNPV HNGHALLMQD THKQLLERGY RRPVLLLHPL GGWTKDDDVP
     LMWRMKQHAA VLEEGVLNPE TTVVAIFPSP MMYAGPTEVQ WHCRARMVAG ANFYIVGRDP
     AGMPHPETGK DLYEPSHGAK VLTMAPGLIT LEIVPFRVAA YNKKKKRMDY YDSEHHEDFE
     FISGTRMRKL AREGQKPPEG FMAPKAWTVL MEYYKSLEKA
//