ID   CYSD2_CHRSD             Reviewed;         303 AA.
AC   Q1QUF8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 2;
DE            EC=2.7.7.4;
DE   AltName: Full=Sulfate adenylate transferase 2;
DE            Short=SAT 2;
DE   AltName: Full=ATP-sulfurylase small subunit 2;
GN   Name=cysD2; OrderedLocusNames=Csal_2553;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
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., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-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.
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DR   EMBL; CP000285; ABE59900.1; -; Genomic_DNA.
DR   RefSeq; YP_574599.1; -.
DR   SMR; Q1QUF8; 5-213.
DR   GeneID; 4026134; -.
DR   GenomeReviews; CP000285_GR; Csal_2553.
DR   KEGG; csa:Csal_2553; -.
DR   NMPDR; fig|290398.4.peg.1913; -.
DR   HOGENOM; Q1QUF8; -.
DR   OMA; Q1QUF8; KTSERQG.
DR   BioCyc; CSAL290398:CSAL_2553-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    303       Sulfate adenylyltransferase subunit 2 2.
FT                                /FTId=PRO_0000340193.
SQ   SEQUENCE   303 AA;  35011 MW;  204DC6B0DF5DCFFF CRC64;
     MLSPERQTHL KQLEAESIHI IREVAAEFAN PVMLYSIGKD SSVMLHLARK AFYPGTPPFP
     LMHVNTTWKF KEMIEFRDRM AAEVGMELIE HINEEGRAAG INPFDHGSAK YTDVMKTQSL
     KQALDKYGFD AAFGGARRDE EASRAKERVY SFRDKHHRWD PKSQRPELWN IYNGKVQKGE
     SIRVFPLSNW TELDIWQYIY LESIPIVPLY YAAPRPVVER DGMQIMVDDE RLPLEDGEVP
     EEKWVRFRTL GCYPLTGAVE STAATLPEII QEMLLTRTSE RSGRAIDHDQ AGSMERKKRE
     GYF
//