ID   CYSD_GEOSM              Reviewed;         301 AA.
AC   C6E751;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=GM21_1864;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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; CP001661; ACT17917.1; -; Genomic_DNA.
DR   RefSeq; WP_015837162.1; NC_012918.1.
DR   AlphaFoldDB; C6E751; -.
DR   SMR; C6E751; -.
DR   STRING; 443144.GM21_1864; -.
DR   EnsemblBacteria; ACT17917; ACT17917; GM21_1864.
DR   KEGG; gem:GM21_1864; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_7; -.
DR   OMA; LMIDTGH; -.
DR   UniPathway; UPA00140; UER00204.
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"
FT                   /id="PRO_1000202401"
SQ   SEQUENCE   301 AA;  34878 MW;  773BF38F08BDF258 CRC64;
     MTTQLTHLQQ LEAESIHIIR EVVAEFDNPV MLYSIGKDSA VMLHLARKAF YPAPPPFPLL
     HVDTTWKFRD MIEFRGRMAK ESGMELLVHV NEEGVKRGVS PFTHGSALYT DVMKTEGLKQ
     ALDRYKFDAA FGGARRDEEK SRAKERIFSF RSANHRWDPK NQRPELWSLY NTRIKPGESI
     RVFPLSNWTE LDIWQYIHLE EIPIVPLYYA AVRPVVERDG MLIMVDDDRL ELKPGEKVEH
     KSVRFRTLGC YPLTGAVESE ADTLPEIIQE MLLTRTSERQ GRLIDHDQAG SMEKKKQEGY
     F