ID CYSC_MICAN Reviewed; 181 AA. AC B0JL16; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 16-JUN-2009, entry version 8. DE RecName: Full=Adenylyl-sulfate kinase; DE EC=2.7.1.25; DE AltName: Full=APS kinase; DE AltName: Full=Adenosine-5'-phosphosulfate kinase; DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase; GN Name=cysC; OrderedLocusNames=MAE_31330; OS Microcystis aeruginosa (strain NIES-843). OC Bacteria; Cyanobacteria; Chroococcales; Microcystis. OX NCBI_TaxID=449447; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18192279; DOI=10.1093/dnares/dsm026; RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., RA Watanabe M.M.; RT "Complete genomic structure of the bloom-forming toxic cyanobacterium RT Microcystis aeruginosa NIES-843."; RL DNA Res. 14:247-256(2007). CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'- CC phosphoadenylyl sulfate. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 2/3. CC -!- SIMILARITY: Belongs to the APS kinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009552; BAG02955.1; -; Genomic_DNA. DR RefSeq; YP_001658147.1; -. DR GeneID; 5863950; -. DR GenomeReviews; AP009552_GR; MAE_31330. DR KEGG; mar:MAE_31330; -. DR OMA; B0JL16; IITITAF. DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP. DR HAMAP; MF_00065; -; 1. DR InterPro; IPR002891; APS_kinase_C. DR Pfam; PF01583; APS_kinase; 1. DR ProDom; PD002350; APS_kinase; 1. DR TIGRFAMs; TIGR00455; apsK; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Phosphoprotein; Transferase. FT CHAIN 1 181 Adenylyl-sulfate kinase. FT /FTId=PRO_1000075086. FT NP_BIND 12 19 ATP (By similarity). FT ACT_SITE 86 86 Phosphoserine intermediate (By FT similarity). SQ SEQUENCE 181 AA; 20110 MW; F577C482D0D63DC2 CRC64; MKQRGVTVWL TGLSGAGKST ITEALQAKLI AEGYSIEVLD GDIVRTNLTK GLGFSKEDRD ENIRRIGFVS NLLTRHGVIV LVSAISPYRE IREEVRGKIG NFVEVFVNAP LSVCEDRDVK GLYKRARAGE IKSFTGIDDP YEPPFNPEVE CRTDLETLEE SVAKVWNKLT ELGYIHQAVA V //