ID CYSD_MARMM Reviewed; 303 AA. AC Q0ALV0; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 2. 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=Mmar10_2451; OS Maricaulis maris (strain MCS10). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Maricaulis. OX NCBI_TaxID=394221; 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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Viollier P., Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-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; CP000449; ABI66743.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_757681.1; -. DR SMR; Q0ALV0; 28-232. DR GeneID; 4285433; -. DR GenomeReviews; CP000449_GR; Mmar10_2451. DR KEGG; mmr:Mmar10_2451; -. DR NMPDR; fig|394221.5.peg.2402; -. DR HOGENOM; Q0ALV0; -. 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 1 303 Sulfate adenylyltransferase subunit 2. FT /FTId=PRO_0000340199. SQ SEQUENCE 303 AA; 35011 MW; 5E23D66C09F5B242 CRC64; MRARPLSAHL KALEAESMHI MREVAAEFDN PVMLYSIGKD SAVMLHLALK AFYPSRPPFP LQHVDSTFKF KEMITFRDAI AEELGLEIRV EINEDGRARG INPFDHGSQL HTQVMKTEAL RSAMTRHKYD AAFGGARRDE EKSRAKERIF SFRDTNHGWD PKNQRPELWS NYNTKIKQGE SIRVFPLSNW TELDIWQYIL EEDIPIVPLY YAAHRPVVER DGQLIMVDDE RLPMKDGEKP DLKLVRFRTL GCYPLTGAIE SSAQTLEEIV LEMLTARTSE RSGRLIDHDE SGSMEKKKRE GYF //