ID CYSC_SHISS Reviewed; 201 AA. AC Q3YYB2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 23. 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=SSON_2898; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). 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; CP000038; AAZ89500.1; -; Genomic_DNA. DR RefSeq; YP_311735.1; -. DR GeneID; 3667603; -. DR GenomeReviews; CP000038_GR; SSON_2898. DR KEGG; ssn:SSON_2898; -. DR HOGENOM; Q3YYB2; -. DR OMA; Q3YYB2; IITITAF. DR BioCyc; SSON300269:SSO_2898-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 1 201 Adenylyl-sulfate kinase. FT /FTId=PRO_1000009035. FT NP_BIND 35 42 ATP (By similarity). FT ACT_SITE 109 109 Phosphoserine intermediate (By FT similarity). SQ SEQUENCE 201 AA; 22321 MW; 11E15BB8F9D2FD4B CRC64; MALHDENVVW HSHPVTVQQR ELHHGHRGVV LWFTGLSGSG KSTVAGALEE ALHKLGVSTY LLDGDNVRHG LCSDLGFSDA DRKENIRRVG EVANLMVEAG LVVLTAFISP HRAERQMVRE RVGEGRFIEV FVDTPLAICE ARDPKGLYKK ARAGELRNFT GIDSVYEAPE SAEIHLNGEQ LVTNLVQQLL DLLRQNDIIR S //