ID   CYSD_PSE14              Reviewed;         305 AA.
AC   Q48ED3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=PSPPH_4133;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ35686.1; -; Genomic_DNA.
DR   RefSeq; YP_276255.1; -.
DR   GeneID; 3558279; -.
DR   GenomeReviews; CP000058_GR; PSPPH_4133.
DR   KEGG; psp:PSPPH_4133; -.
DR   NMPDR; fig|264730.3.peg.4531; -.
DR   HOGENOM; Q48ED3; -.
DR   OMA; Q48ED3; SLRVFPL.
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    305       Sulfate adenylyltransferase subunit 2.
FT                                /FTId=PRO_1000008965.
SQ   SEQUENCE   305 AA;  35312 MW;  93CE76EA132C89C8 CRC64;
     MVDKLTHLKQ LEAESIHIIR EVAAEFDNPV MLYSIGKDSA VMLHLARKAF FPGKLPFPVM
     HVDTRWKFQE MYRFRDKMVE EMGLDLITHI NPDGVAQGIN PFTHGSAKHT DIMKTEGLKQ
     ALDKHGFDAA FGGARRDEEK SRAKERVYSF RDSKHRWDPK NQRPELWNVY NGNVNKGESI
     RVFPLSNWTE LDIWQYIYLE GIPIVPLYFA AERDVIEKNG TLIMIDDERI LEHLTDEEKS
     RIVKKKVRFR TLGCYPLTGA VESEATSLTD IIQEMLLTRT SERQGRVIDH DGAGSMEEKK
     RQGYF
//