ID CYSD_ECOL5 Reviewed; 302 AA. AC Q0TEA6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Sulfate adenylyltransferase subunit 2; DE EC=2.7.7.4; DE AltName: Full=Sulfate adenylate transferase; DE Short=SAT; DE AltName: Full=ATP-sulfurylase small subunit; GN Name=cysD; OrderedLocusNames=ECP_2734; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl CC sulfate. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 1/3. CC -!- SUBUNIT: Heterodimer composed of cysD, the smaller subunit, and CC cysN (By similarity). CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily. 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; CP000247; ABG70723.1; -; Genomic_DNA. DR RefSeq; YP_670624.1; -. DR SMR; Q0TEA6; 5-212. DR GeneID; 4191559; -. DR GenomeReviews; CP000247_GR; ECP_2734. DR KEGG; ecp:ECP_2734; -. DR NMPDR; fig|340197.3.peg.1316; -. DR HOGENOM; Q0TEA6; -. DR OMA; Q0TEA6; KTSERQG. DR BioCyc; ECOL362663:ECP_2734-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:HAMAP. DR GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP. DR GO; GO:0019419; P:sulfate reduction; IEA:InterPro. DR HAMAP; MF_00064; -; 1. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011784; SO4_adenylTrfase_ssu. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF01507; PAPS_reduct; 1. DR PIRSF; PIRSF002936; CysDAde_trans; 1. DR TIGRFAMs; TIGR02039; CysD; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Nucleotidyltransferase; Transferase. FT CHAIN 1 302 Sulfate adenylyltransferase subunit 2. FT /FTId=PRO_1000008956. SQ SEQUENCE 302 AA; 35202 MW; 005AC9C26FC88B60 CRC64; MDQKRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR INLQPGEVIK KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG YF //