ID   CYSD_ECOUT              Reviewed;         302 AA.
AC   Q1R7T9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
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=UTI89_C3123;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE08575.1; -; Genomic_DNA.
DR   RefSeq; YP_542106.1; -.
DR   SMR; Q1R7T9; 5-212.
DR   GeneID; 3990448; -.
DR   GenomeReviews; CP000243_GR; UTI89_C3123.
DR   KEGG; eci:UTI89_C3123; -.
DR   HOGENOM; Q1R7T9; -.
DR   OMA; Q1R7T9; KTSERQG.
DR   BioCyc; ECOL364106:UTI89_C3123-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_1000008957.
SQ   SEQUENCE   302 AA;  35192 MW;  AF5AC9C0BD1889B2 CRC64;
     MDQKRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL
     LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK
     QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES
     IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR INLQSGEVIK
     KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG
     YF
//