ID   CYSD_SHEHH              Reviewed;         302 AA.
AC   B0TTD5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Shal_3533;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ78076.1; -; Genomic_DNA.
DR   RefSeq; WP_012278596.1; NC_010334.1.
DR   AlphaFoldDB; B0TTD5; -.
DR   SMR; B0TTD5; -.
DR   STRING; 458817.Shal_3533; -.
DR   EnsemblBacteria; ABZ78076; ABZ78076; Shal_3533.
DR   KEGG; shl:Shal_3533; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OMA; MMILAED; -.
DR   OrthoDB; 499077at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001317; 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_1000075083"
SQ   SEQUENCE   302 AA;  35097 MW;  5F04B57D782BD9BC CRC64;
     MAAKELSHLQ QLEAESIQII REVAAEFDNP VMMYSIGKDS SVMLHLARKA FYPGKIPFPL
     LHVDTDWKFK EMIAFRDEQA KEFGFELLVH KNPEGLEMGI SPFEHGSAKH TDIMKTQGLK
     QALNKYGFDA AFGGARRDEE KSRAKERVYS FRDKHHTWDP KNQRPELWRT YNGAVNKGES
     IRVFPLSNWT ELDIWQYIYQ ENIQLVPLYF AQKRPVVERD GMMIMVDDDR MPLAEGEQPK
     QELVRFRTLG CYPLTGAMHS EADTLEKIIE EMLLTRSSER QGRLIDSDQS ASMELKKRQG
     YF