ID CYSC_BUCAP Reviewed; 211 AA. AC Q8K9D4; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 48. 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=BUsg_407; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; AE013218; AAM67957.1; -; Genomic_DNA. DR RefSeq; NP_660746.1; -. DR HSSP; Q12657; 1M7G. DR GeneID; 1005753; -. DR GenomeReviews; AE013218_GR; BUsg_407. DR KEGG; bas:BUsg407; -. DR HOGENOM; Q8K9D4; -. DR OMA; Q8K9D4; IITITAF. DR BioCyc; BAPH198804:BUSG407-MON; -. 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 1 211 Adenylyl-sulfate kinase. FT /FTId=PRO_0000105906. FT NP_BIND 36 43 ATP (Potential). FT ACT_SITE 110 110 Phosphoserine intermediate (By FT similarity). SQ SEQUENCE 211 AA; 24288 MW; 0644BA855D76B6B1 CRC64; MHNNSKKNII WQKHSVTRIK REQKNGHKSI VIWFTGLSGS GKSSIANSLE EILFQNNFNT YLLDGDNIRS SLCSDLSFSI LDRNENIRRI GEVSKLMIDA GIIVLVSVIS PYRNQRKKIR LMLGKINFLE VFVDTPLNIC EERDPKKLYQ KSRLGKISDL TGIQSLYEIP EKPDLHLDET ISLKNNTKKL IHILCDKNII SFPNIDETFL F //