ID   CYSD2_ALHEH             Reviewed;         302 AA.
AC   Q0A653;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Mlg_2344;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
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.
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DR   EMBL; CP000453; ABI57684.1; -; Genomic_DNA.
DR   RefSeq; YP_743174.1; -.
DR   SMR; Q0A653; 6-212.
DR   GeneID; 4269100; -.
DR   GenomeReviews; CP000453_GR; Mlg_2344.
DR   KEGG; aeh:Mlg_2344; -.
DR   NMPDR; fig|187272.6.peg.2228; -.
DR   HOGENOM; Q0A653; -.
DR   OMA; Q0A653; 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    302       Sulfate adenylyltransferase subunit 2 2.
FT                                /FTId=PRO_0000340176.
SQ   SEQUENCE   302 AA;  35141 MW;  981C33BA9F957E8A CRC64;
     MDNRTLTHLR QLEAESIHII REVVAEFENP VMLYSIGKDS SVMLHLARKA FYPGTPPFPL
     MHVDTTWKFR EMIEFRDRMA KEAGMELIVH INQEGVAQGI GPFSHGSRVH TDVMKTQSLK
     QALDKYRFDA AFGGARRDEE RSRAKERVYS FRDRNHAWDP KNQRPELWRL YNGQVHKGES
     IRVFPLSNWT ELDIWQYIYL EEIPIVPLYY AARRPVVERD GTLIMVDDDR MPLEPGEEPE
     MAMVRFRTLG CYPLTGAIRS EAATLPEIIQ EMLLTKSSER QGRVIDHDAA GSMEEKKRQG
     YF
//