ID   CYSD2_SHESH             Reviewed;         301 AA.
AC   A8FXM2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 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 2 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase 2 {ECO:0000255|HAMAP-Rule:MF_00064};
DE            Short=SAT 2 {ECO:0000255|HAMAP-Rule:MF_00064};
GN   Name=cysD2 {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=Ssed_2988;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000821; ABV37595.1; -; Genomic_DNA.
DR   RefSeq; WP_012143325.1; NC_009831.1.
DR   AlphaFoldDB; A8FXM2; -.
DR   SMR; A8FXM2; -.
DR   STRING; 425104.Ssed_2988; -.
DR   EnsemblBacteria; ABV37595; ABV37595; Ssed_2988.
DR   KEGG; sse:Ssed_2988; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OMA; SQWDPRR; -.
DR   OrthoDB; 499077at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002015; 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..301
FT                   /note="Sulfate adenylyltransferase subunit 2 2"
FT                   /id="PRO_0000340221"
SQ   SEQUENCE   301 AA;  34787 MW;  3932EF9DCA29FE14 CRC64;
     MSKYQTHLKQ LEAESIQIMR EVAAEFDNPV MLYSVGKDSS VLLHLARKAF YPGKIPFPLM
     HVDTNWKFKE MIDFRDKMAK KHGFDLIVHK NPRGMEMGVG PFTHGSAKHT DIMKTEGLKQ
     ALDMHGFDAA FGGARRDEEK SRAKERVYSF RDSKHRWDPK NQRPELWNIY NGKVDKGESI
     RVFPLSNWTE LDIWQYIYLE GIEIPSLYLA AERPVVERDG TLIMVDDERM PIEEGEKVEN
     KMVRFRTLGC YPLTGAVESQ AQTLPEIIQE MLLCTTSERQ GRVIDNDSAG SMEKKKMEGY
     F