ID   CYSD1_CHRSD             Reviewed;         305 AA.
AC   Q1QWX0;
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 1;
DE            EC=2.7.7.4;
DE   AltName: Full=Sulfate adenylate transferase 1;
DE            Short=SAT 1;
DE   AltName: Full=ATP-sulfurylase small subunit 1;
GN   Name=cysD1; OrderedLocusNames=Csal_1686;
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; ABE59038.1; -; Genomic_DNA.
DR   RefSeq; YP_573737.1; -.
DR   SMR; Q1QWX0; 7-215.
DR   GeneID; 4028698; -.
DR   GenomeReviews; CP000285_GR; Csal_1686.
DR   KEGG; csa:Csal_1686; -.
DR   NMPDR; fig|290398.4.peg.2097; -.
DR   HOGENOM; Q1QWX0; -.
DR   OMA; Q1QWX0; SLRVFPL.
DR   BioCyc; CSAL290398:CSAL_1686-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    305       Sulfate adenylyltransferase subunit 2 1.
FT                                /FTId=PRO_0000340192.
SQ   SEQUENCE   305 AA;  35196 MW;  7090AE4282FACDF4 CRC64;
     MSGITPERQT HLKQLEAESI HIIREVAAEF ANPVMLYSIG KDSSVMLHLA RKAFYPGTPP
     FPLMHVNTTW KFKEMIEFRD RMAAEVGMEL IEHINEEGRA AGINPFDHGS AKYTDVMKTQ
     SLKQALDKYG FDAAFGGARR DEEASRAKER VYSFRDKHHR WDPKNQRPEL WNIYNGKVQK
     GESIRVFPLS NWTELDIWQY IYLESIPIVP LYYAAPRPVV ERDGMQIMVD DERLPLEDGE
     VPEEKWVRFR TLGCYPLTGA VESTAATLPE IIQEMLLTRT SERSGRAIDH DQAGSMERKK
     REGYF
//