ID CYSD_RHIEC Reviewed; 317 AA. AC Q2KB48; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=RHE_CH01131; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000133; ABC89938.1; -; Genomic_DNA. DR RefSeq; YP_468665.1; -. DR SMR; Q2KB48; 23-226. DR GeneID; 3890641; -. DR GenomeReviews; CP000133_GR; RHE_CH01131. DR KEGG; ret:RHE_CH01131; -. DR HOGENOM; Q2KB48; -. DR OMA; Q2KB48; NITPFTH. 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 1 317 Sulfate adenylyltransferase subunit 2. FT /FTId=PRO_1000008976. SQ SEQUENCE 317 AA; 36510 MW; E9028E53E15C8301 CRC64; MPDSRPDTEL SNPQSAKAPL DPHLKALENE SIHIFREVAA EFERPVMLYS IGKDSSVLLH LARKAFYPGR VPFPLLHVNT GWKFREMIAF RDETARKYDL DLIEHINPRG AAENITPFTH GSAAFTDIMK TESLRQALDA GQFDAAFGGA RRDEEASRAK ERIYSFRTPD HRWDPRNQRP ELWNIYNGMI RKGESVRAFP LSNWTEVDIW RYIQAEDIPL VPLYYAKKRK FVERDGMMIL AEDPRLELLP GEVRQEGMIR FRTLGDFPLT GAIRSQATTL EEVIAELEIA TVSERQGRAI DRDQSGSMEK KKREGYF //