ID CYSD_PSEPF Reviewed; 305 AA. AC Q3KHY6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 31. 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=Pfl01_0877; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) 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; CP000094; ABA72620.1; -; Genomic_DNA. DR RefSeq; YP_346609.1; -. DR GeneID; 3715668; -. DR GenomeReviews; CP000094_GR; Pfl01_0877. DR KEGG; pfo:Pfl01_0877; -. DR HOGENOM; Q3KHY6; -. DR OMA; Q3KHY6; SLRVFPL. DR BioCyc; PFLU205922:PFL_0877-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 1 305 Sulfate adenylyltransferase subunit 2. FT /FTId=PRO_1000008972. SQ SEQUENCE 305 AA; 35321 MW; 15EA8FE9B293C7FE CRC64; MVDKLTHLKQ LEAESIHIIR EVAAEFDNPV MLYSIGKDSA VMLHLARKAF FPGKLPFPVM HVDTRWKFQE MYKFRDKMVE ELGLDLITHI NPDGVAQNIN PFTHGSAKHT DIMKTEGLKQ ALDKHGFDAA FGGARRDEEK SRAKERVYSF RDSKHRWDPK NQRPELWNVY NGKVNKGESI RVFPLSNWTE LDIWQYIYLE GIPIVPLYFA AEREVIEKNG TLIMIDDERI LEHLSDEDKA RIVKKKVRFR TLGCYPLTGA VESEAESLTD IIQEMLLTRT SERQGRVIDH DGAGSMEDKK RQGYF //