ID   CYSD_HYPNA              Reviewed;         328 AA.
AC   Q0C438;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=HNE_0777;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(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; CP000158; ABI77512.1; -; Genomic_DNA.
DR   RefSeq; YP_759505.1; -.
DR   SMR; Q0C438; 32-238.
DR   GeneID; 4289582; -.
DR   GenomeReviews; CP000158_GR; HNE_0777.
DR   KEGG; hne:HNE_0777; -.
DR   NMPDR; fig|228405.5.peg.760; -.
DR   TIGR; HNE_0777; -.
DR   HOGENOM; Q0C438; -.
DR   OMA; Q0C438; AKERVIS.
DR   BioCyc; HNEP81032:HNE_0777-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    328       Sulfate adenylyltransferase subunit 2.
FT                                /FTId=PRO_0000340197.
SQ   SEQUENCE   328 AA;  37535 MW;  042F0C503BB1AA0A CRC64;
     MRTRHGAFLL LARPATERAH TPEQDQYTLP TLTHLDRLEA ESLHILREVA AECEKPVMLY
     SIGKDSAVML HLAMKAFYPA RPPFPLLHVD TGWKFREMIA FRDRKVKELG LELLVHMNED
     GVREGVGPFT HGSAYHTDVM KTAALKQALD KYGFDAAFGG ARRDEEKSRA KERVISFRSA
     GHRWDPKRQR PEIWNLYNTR MHKGESLRAF PLSNWTELDI WQYIRREGIE LVPLYLAAPR
     PVVTWNDTLI MVDDDRVPAE IAAKAEVKSV RFRTLGCYPL TGAVESTATT LDDVIQEILL
     TTTSERQGRA IDKDQTASME KKKQEGYF
//