ID   CYSD_CROS8              Reviewed;         302 AA.
AC   A7MJ68;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00064};
DE            EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=ATP-sulfurylase small subunit {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00064};
DE            Short=SAT {ECO:0000255|HAMAP-Rule:MF_00064};
GN   Name=cysD {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=ESA_00539;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC       adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC       diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC       APS synthesis involves the formation of a high-energy phosphoric-
CC       sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC       to ATP hydrolysis by CysD. {ECO:0000255|HAMAP-Rule:MF_00064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00064};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00064}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000255|HAMAP-Rule:MF_00064}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00064}.
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DR   EMBL; CP000783; ABU75830.1; -; Genomic_DNA.
DR   RefSeq; WP_004387918.1; NC_009778.1.
DR   AlphaFoldDB; A7MJ68; -.
DR   SMR; A7MJ68; -.
DR   EnsemblBacteria; ABU75830; ABU75830; ESA_00539.
DR   GeneID; 45714387; -.
DR   GeneID; 56729439; -.
DR   GeneID; 60762532; -.
DR   KEGG; esa:ESA_00539; -.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OMA; LMIDTGH; -.
DR   OrthoDB; 499077at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
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; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..302
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_1000008958"
SQ   SEQUENCE   302 AA;  35181 MW;  CECF322D184B8397 CRC64;
     MDQKRLTHLR QLEAESIHII REVAAEFANP VMMYSIGKDS SVMLHLARKA FYPGTLPFPL
     LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK
     QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES
     IRVFPLSNWT ELDIWQYIYL ENIEIVPLYL AAERPVLERD GMLMMIDDDR IDLQPGEEIK
     PRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG
     YF