ID CYSD_HAHCH Reviewed; 302 AA. AC Q2SBG0; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=HCH_05342; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., RA Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., RA Park H.-S., Lee H.K., Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing RT an algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). 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; CP000155; ABC32014.1; -; Genomic_DNA. DR RefSeq; YP_436439.1; -. DR SMR; Q2SBG0; 6-212. DR GeneID; 3838700; -. DR GenomeReviews; CP000155_GR; HCH_05342. DR KEGG; hch:HCH_05342; -. DR NMPDR; fig|349521.5.peg.4693; -. DR HOGENOM; Q2SBG0; -. DR OMA; Q2SBG0; KTSERQG. DR BioCyc; HCHE349521:HCH_05342-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_0000340196. SQ SEQUENCE 302 AA; 34995 MW; 2686D64F45BC44D7 CRC64; MTDYNLTHLK QLEAESIHII REVAAEFERP VMLYSIGKDS SVMLHLARKA FFPGKPPFPL MHVDTTWKFQ DMITFRDQQA AKFGLDLIVH INEDGVRQGI GPFTHGSAKH TDVMKTESLK QALNKYKFDA AFGGARRDEE KSRAKERVYS FRDSNHRWDP KNQRPELWNL YNGKINKGES IRVFPLSNWT ELDIWQYIYL ENIELVPLYF SAKRPVVERD GTMIMVDDDR MPLKPGETPM MKDVRFRTLG CYPLTGAIES TATTLPEIIQ EMLLTTSSER QGRVIDHDQA GSMEQKKREG YF //