ID CYSC_SHIF8 Reviewed; 201 AA. AC Q0T1I1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 18. 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=SFV_2748; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(2006). 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; CP000266; ABF04834.1; -; Genomic_DNA. DR RefSeq; YP_690139.1; -. DR GeneID; 4210398; -. DR GenomeReviews; CP000266_GR; SFV_2748. DR KEGG; sfv:SFV_2748; -. DR HOGENOM; Q0T1I1; -. DR OMA; Q0T1I1; IITITAF. DR BioCyc; SFLE373384:SFV_2748-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_1000009033. 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 //