ID   CYSD_RHIL3              Reviewed;         317 AA.
AC   Q1MJV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-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=RL1261;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:RESEARCH34.1-RESEARCH34.20(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.
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DR   EMBL; AM236080; CAK06757.1; -; Genomic_DNA.
DR   RefSeq; YP_766866.1; -.
DR   SMR; Q1MJV3; 23-226.
DR   GeneID; 4401829; -.
DR   GenomeReviews; AM236080_GR; RL1261.
DR   KEGG; rle:RL1261; -.
DR   NMPDR; fig|216596.1.peg.1314; -.
DR   HOGENOM; Q1MJV3; -.
DR   OMA; Q1MJV3; 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_1000008977.
SQ   SEQUENCE   317 AA;  36409 MW;  2AF98262070697AC CRC64;
     MPDSRPDTEL SNPQSAKAPL DPHLKALENE SIHIFREVAA EFERPVMLYS IGKDSSVLLH
     LARKAFYPGR VPFPLLHVNT GWKFSEMIAF RDETAKKYDL DLIEHINPRG KAENITPFTH
     GSAAFTDIMK TEGLRQALDA GQFDAAFGGA RRDEEASRAK ERIYSFRTPD HRWDPRNQRP
     ELWNIYNGMI RKGESVRAFP LSNWTEVDIW RYIQAEDIPL VPLYYAKKRP FVERDGMMIL
     AEDPRLELLP GEVRQEGMIR FRTLGDFPLT GAIRSQATTL EEVIAELEIA TVSERQGRAI
     DRDQSGSMEK KKREGYF
//