ID   R0GZZ7_9BRAS            Unreviewed;       289 AA.
AC   R0GZZ7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
DE            EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|RuleBase:RU004347};
GN   ORFNames=CARUB_v10006314mg {ECO:0000313|EMBL:EOA17905.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA17905.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|RuleBase:RU004347}.
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:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
CC       {ECO:0000256|RuleBase:RU004347}.
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; KB870811; EOA17905.1; -; Genomic_DNA.
DR   RefSeq; XP_006285007.1; XM_006284945.1.
DR   AlphaFoldDB; R0GZZ7; -.
DR   STRING; 81985.R0GZZ7; -.
DR   GeneID; 17880147; -.
DR   KEGG; crb:17880147; -.
DR   eggNOG; KOG0635; Eukaryota.
DR   OrthoDB; 642041at2759; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd02027; APSK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR11055:SF53; ADENYLYL-SULFATE KINASE 2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004347};
KW   Kinase {ECO:0000256|RuleBase:RU004347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ   SEQUENCE   289 AA;  31895 MW;  BF1F7787540359EA CRC64;
     MEGLAIRASR PSVFYSLPGL GGDSQRRRPS SDGFLKLPAE NRKIIANSAS FHPISAVNVS
     AQASLTADFP ALSETSLEER RINGKEKAEN IVWHESSICR CDRQQLLQQK GCVIWITGLS
     GSGKSTVACA LSKALFERGK LTYTLDGDNV RHGLNRDLTF KTEDRTENIR RIGEVAKLFA
     DVGVICIASL ISPYRRDRDA CRSLLPEGDF VEVFMDVPLH VCESRDPKGL YKLARAGKIK
     GFTGIDDPYE APLNCEVVLK HTGDEDSCSP RQMAENIISY LQNKGYLEG
//