ID   CYSD1_ALHEH             Reviewed;         315 AA.
AC   Q0A977;
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 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=Mlg_1261;
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; ABI56610.1; -; Genomic_DNA.
DR   RefSeq; YP_742100.1; -.
DR   SMR; Q0A977; 20-225.
DR   GeneID; 4269183; -.
DR   GenomeReviews; CP000453_GR; Mlg_1261.
DR   KEGG; aeh:Mlg_1261; -.
DR   NMPDR; fig|187272.6.peg.1209; -.
DR   HOGENOM; Q0A977; -.
DR   OMA; Q0A977; MIFGGAR.
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    315       Sulfate adenylyltransferase subunit 2 1.
FT                                /FTId=PRO_0000340175.
SQ   SEQUENCE   315 AA;  35674 MW;  A03A6FBFC60F3B05 CRC64;
     MSSAATALQG PQPNALPAAS HLDRLEAESI HILREVAAEF DNPVMLYSVG KDSSVMLHLA
     RKAFHPGTPP FPLLHVDTTW KFREMIAFRD RMAAESGMAL RVHINQEGVA RGIGPFSHGS
     AVHTDVMKTQ ALKQALDRYG FDAAFGGARR DEEASRAKER VYSFRDRHHR WDPKAQRPEL
     WNVYNGRIHK GESIRVFPLS NWTELDIWLY IHREGIPVVP LYFAAERPVV ERDGLLIMVD
     DDRLPLAPGE IPRLERVRFR TLGCYPLTGA IRSEARSVPE IIAEMLDSSS SERQGRAIDH
     DQSGSMERKK REGYF
//