ID CYSD_RHOP5 Reviewed; 328 AA. AC Q07UU1; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 20. 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=RPE_0334; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316055; 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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., Kim E., RA Harwood C.S., Oda Y., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000463; ABJ04293.1; -; Genomic_DNA. DR RefSeq; YP_779273.1; -. DR SMR; Q07UU1; 33-238. DR GeneID; 4360002; -. DR GenomeReviews; CP000463_GR; RPE_0334. DR KEGG; rpe:RPE_0334; -. DR HOGENOM; Q07UU1; -. DR OMA; Q07UU1; SLRVFPL. 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 1 328 Sulfate adenylyltransferase subunit 2. FT /FTId=PRO_0000340216. SQ SEQUENCE 328 AA; 37000 MW; 97119D0039A2D0E7 CRC64; MSDILDYPDV SSPAAAPDLA DLGGEPARAR PSSHLQRLES ESIHILREVA AEFRKPVMLY SIGKDSSVLL HLAMKAFAPG KPPFPLLHVD TTWKFREMIA FRDQRIRELG LDLLVHVNPD GVAQRVGPFS HGSARHTDVM KTQALRQALD AHGFDAAIGG ARRDEEKSRA KERIFSHRSA AHRWDPKNQR PELWSLYNTM LAPGESMRVF PLSNWTELDI WDYILIERIP IVPLYFAAER PVVERDGALI LVDDERMPLR PGEVPQWRSV RFRTLGCYPL TGAVPSTATT LPAIVQEMMA SRSSEREGRV IDRDSTASME RKKAEGYF //