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Database: UniProt
Entry: A0A2K6BMR0_MACNE
LinkDB: A0A2K6BMR0_MACNE
Original site: A0A2K6BMR0_MACNE 
ID   A0A2K6BMR0_MACNE        Unreviewed;       580 AA.
AC   A0A2K6BMR0;
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:ENSMNEP00000012706.1};
GN   Name=PAPSS1 {ECO:0000313|Ensembl:ENSMNEP00000012706.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000012706.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000012706.1}
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; A0A2K6BMR0; -.
DR   Ensembl; ENSMNET00000036903.1; ENSMNEP00000012706.1; ENSMNEG00000030623.1.
DR   GeneTree; ENSGT00390000009613; -.
DR   OMA; LVYEGCR; -.
DR   UniPathway; UPA00097; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000030623; Expressed in temporal lobe 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:UP000233120};
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;  65858 MW;  B7FE79EC55149D00 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 QWGTTCRNHP 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
//
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