ID   CYSD_COLP3              Reviewed;         299 AA.
AC   Q483A0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=CPS_2142;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ26896.1; -; Genomic_DNA.
DR   RefSeq; YP_268867.1; -.
DR   SMR; Q483A0; 3-208.
DR   GeneID; 3521151; -.
DR   GenomeReviews; CP000083_GR; CPS_2142.
DR   KEGG; cps:CPS_2142; -.
DR   NMPDR; fig|167879.3.peg.2085; -.
DR   TIGR; CPS_2142; -.
DR   HOGENOM; Q483A0; -.
DR   OMA; Q483A0; KTSERQG.
DR   BioCyc; CPSY167879:CPS_2142-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    299       Sulfate adenylyltransferase subunit 2.
FT                                /FTId=PRO_0000340194.
SQ   SEQUENCE   299 AA;  34406 MW;  48EC8E1C0F03BE63 CRC64;
     MNLTHLKTLE AESIHIFREV AAEFDNPVML YSVGKDSAVL LHLARKAFAP GKIPFPLLHV
     DTNWKFKEMI AFRDQMAKDY DFELLVHKNP EGIEMGMGPF THGSATHTDV MKTQGLKQAL
     NKYGFDAAFG GARRDEEKSR AKERVYSFRD ENHRWDPKSQ RPELWNIYNG KVNKGESIRV
     FPLSNWTELD IWQYIYLESI PIVPLYLAEK RPVVERDGTL IMVDDDRMPI GEDEEVQMKS
     VRFRTLGCYP LTGAVESTAN TLPEIIQEML LTKTSERQGR VIDHDSAGSM EKKKMEGYF
//