ID CYSC_SHESR Reviewed; 205 AA. AC Q0HYA3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 20. 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=Shewmr7_0903; OS Shewanella sp. (strain MR-7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., RA Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate. 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; CP000444; ABI41902.1; -; Genomic_DNA. DR RefSeq; YP_736959.1; -. DR GeneID; 4257426; -. DR GenomeReviews; CP000444_GR; Shewmr7_0903. DR KEGG; shm:Shewmr7_0903; -. DR NMPDR; fig|60481.10.peg.867; -. DR HOGENOM; Q0HYA3; -. DR OMA; Q0HYA3; IVWHQHS. 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 1 205 Adenylyl-sulfate kinase. FT /FTId=PRO_1000009029. FT NP_BIND 31 38 ATP (By similarity). FT ACT_SITE 105 105 Phosphoserine intermediate (By FT similarity). SQ SEQUENCE 205 AA; 22381 MW; 46AB07AA57531100 CRC64; MSNIVWHQHS VDQADRAKLK GQNPVLLWFT GLSGAGKSTL AGALERALFD AGFHTYLLDG DNVRHGLCKD LGFSVADRDE NLRRVGEVAK LMVDAGLVVL SAFISPTREE RDSIRARFPE GQFIEVHVST PLSICEQRDP KGLYVKARRG EISNFTGISS PYEAPLSAEL TIDTSKGDLA SQVRALIDYL TAIEVINPSR LTASA //